Squire Booker: Difference between revisions
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Booker is a professor of biology, biochemistry, and molecular biology at Penn State University.<ref name=":0" /><ref name=":1" /> His research explores how enzymes change their catalytic abilities due to metal ions or metal clusters.<ref>{{Citation|last=Elango|first=B.|chapter=United States Service Sector Data|date=2015|title=Service Industry Databook|pages=17–55|publisher=Springer International Publishing|doi=10.1007/978-3-319-19111-9_3|isbn=978-3-319-19110-2}}</ref><ref name=":16">{{Cite journal|last1=Cicchillo|first1=Robert M.|last2=Iwig|first2=David F.|last3=Jones|first3=A. Daniel|last4=Nesbitt|first4=Natasha M.|last5=Baleanu-Gogonea|first5=Camelia|last6=Souder|first6=Matthew G.|last7=Tu|first7=Loretta|last8=Booker|first8=Squire J.|date=June 2004|title=Lipoyl Synthase Requires Two Equivalents ofS-Adenosyl-l-methionine To Synthesize One Equivalent of Lipoic Acid†|journal=Biochemistry|volume=43|issue=21|pages=6378–6386|doi=10.1021/bi049528x|pmid=15157071|issn=0006-2960}}</ref> His research focuses on enzymes containing iron-sulfur clusters which catalyze chemical reactions.<ref name=":0" /><ref name=":12">{{Cite journal|last1=Lieder|first1=Kafryn W.|last2=Booker|first2=Squire|last3=Ruzicka|first3=Frank J.|last4=Beinert|first4=Helmut|last5=Reed|first5=George H.|last6=Frey|first6=Perry A.|date=February 1998|title=S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron−Sulfur Centers by Electron Paramagnetic Resonance†|journal=Biochemistry|volume=37|issue=8|pages=2578–2585|doi=10.1021/bi972417w|pmid=9485408|issn=0006-2960}}</ref><ref name=":17">{{Cite journal|last1=Blaszczyk|first1=Anthony J.|last2=Silakov|first2=Alexey|last3=Zhang|first3=Bo|last4=Maiocco|first4=Stephanie J.|last5=Lanz|first5=Nicholas D.|last6=Kelly|first6=Wendy L.|last7=Elliott|first7=Sean J.|last8=Krebs|first8=Carsten|last9=Booker|first9=Squire J.|date=2016-03-03|title=Spectroscopic and Electrochemical Characterization of the Iron–Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase|journal=Journal of the American Chemical Society|volume=138|issue=10|pages=3416–3426|doi=10.1021/jacs.5b12592|pmid=26841310|issn=0002-7863}}</ref> He focuses on the Radical S-adenosylamethionine Superfamily (SAM) which is a group of enzymes that encounters radical chemistry in post-transcriptional and post-translational modifications of DNA.<ref name=":0" /><ref name=":13">{{Cite journal|last1=Grove|first1=Tyler L.|last2=Lee|first2=Kyung-Hoon|last3=St. Clair|first3=Jennifer|last4=Krebs|first4=Carsten|last5=Booker|first5=Squire J.|date=July 2008|title=In Vitro Characterization of AtsB, a Radical SAM Formylglycine-Generating Enzyme That Contains Three [4Fe-4S] Clusters†|journal=Biochemistry|volume=47|issue=28|pages=7523–7538|doi=10.1021/bi8004297|pmid=18558715|issn=0006-2960|pmc=2664749}}</ref><ref name=":14">{{Cite journal|last1=Chatterjee|first1=Abhishek|last2=Li|first2=Yue|last3=Zhang|first3=Yang|last4=Grove|first4=Tyler L|last5=Lee|first5=Michael|last6=Krebs|first6=Carsten|last7=Booker|first7=Squire J|last8=Begley|first8=Tadhg P|last9=Ealick|first9=Steven E|date=2008-10-26|title=Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily|journal=Nature Chemical Biology|volume=4|issue=12|pages=758–765|doi=10.1038/nchembio.121|pmid=18953358|issn=1552-4450|pmc=2587053}}</ref><ref name=":15">{{Cite journal|last1=Booker|first1=Squire J|last2=Cicchillo|first2=Robert M|last3=Grove|first3=Tyler L|date=October 2007|title=Self-sacrifice in radical S-adenosylmethionine proteins|journal=Current Opinion in Chemical Biology|volume=11|issue=5|pages=543–552|doi=10.1016/j.cbpa.2007.08.028|pmid=17936058|issn=1367-5931|pmc=2637762}}</ref> |
Booker is a professor of biology, biochemistry, and molecular biology at Penn State University.<ref name=":0" /><ref name=":1" /> His research explores how enzymes change their catalytic abilities due to metal ions or metal clusters.<ref>{{Citation|last=Elango|first=B.|chapter=United States Service Sector Data|date=2015|title=Service Industry Databook|pages=17–55|publisher=Springer International Publishing|doi=10.1007/978-3-319-19111-9_3|isbn=978-3-319-19110-2}}</ref><ref name=":16">{{Cite journal|last1=Cicchillo|first1=Robert M.|last2=Iwig|first2=David F.|last3=Jones|first3=A. Daniel|last4=Nesbitt|first4=Natasha M.|last5=Baleanu-Gogonea|first5=Camelia|last6=Souder|first6=Matthew G.|last7=Tu|first7=Loretta|last8=Booker|first8=Squire J.|date=June 2004|title=Lipoyl Synthase Requires Two Equivalents ofS-Adenosyl-l-methionine To Synthesize One Equivalent of Lipoic Acid†|journal=Biochemistry|volume=43|issue=21|pages=6378–6386|doi=10.1021/bi049528x|pmid=15157071|issn=0006-2960}}</ref> His research focuses on enzymes containing iron-sulfur clusters which catalyze chemical reactions.<ref name=":0" /><ref name=":12">{{Cite journal|last1=Lieder|first1=Kafryn W.|last2=Booker|first2=Squire|last3=Ruzicka|first3=Frank J.|last4=Beinert|first4=Helmut|last5=Reed|first5=George H.|last6=Frey|first6=Perry A.|date=February 1998|title=S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron−Sulfur Centers by Electron Paramagnetic Resonance†|journal=Biochemistry|volume=37|issue=8|pages=2578–2585|doi=10.1021/bi972417w|pmid=9485408|issn=0006-2960}}</ref><ref name=":17">{{Cite journal|last1=Blaszczyk|first1=Anthony J.|last2=Silakov|first2=Alexey|last3=Zhang|first3=Bo|last4=Maiocco|first4=Stephanie J.|last5=Lanz|first5=Nicholas D.|last6=Kelly|first6=Wendy L.|last7=Elliott|first7=Sean J.|last8=Krebs|first8=Carsten|last9=Booker|first9=Squire J.|date=2016-03-03|title=Spectroscopic and Electrochemical Characterization of the Iron–Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase|journal=Journal of the American Chemical Society|volume=138|issue=10|pages=3416–3426|doi=10.1021/jacs.5b12592|pmid=26841310|issn=0002-7863}}</ref> He focuses on the Radical S-adenosylamethionine Superfamily (SAM) which is a group of enzymes that encounters radical chemistry in post-transcriptional and post-translational modifications of DNA.<ref name=":0" /><ref name=":13">{{Cite journal|last1=Grove|first1=Tyler L.|last2=Lee|first2=Kyung-Hoon|last3=St. Clair|first3=Jennifer|last4=Krebs|first4=Carsten|last5=Booker|first5=Squire J.|date=July 2008|title=In Vitro Characterization of AtsB, a Radical SAM Formylglycine-Generating Enzyme That Contains Three [4Fe-4S] Clusters†|journal=Biochemistry|volume=47|issue=28|pages=7523–7538|doi=10.1021/bi8004297|pmid=18558715|issn=0006-2960|pmc=2664749}}</ref><ref name=":14">{{Cite journal|last1=Chatterjee|first1=Abhishek|last2=Li|first2=Yue|last3=Zhang|first3=Yang|last4=Grove|first4=Tyler L|last5=Lee|first5=Michael|last6=Krebs|first6=Carsten|last7=Booker|first7=Squire J|last8=Begley|first8=Tadhg P|last9=Ealick|first9=Steven E|date=2008-10-26|title=Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily|journal=Nature Chemical Biology|volume=4|issue=12|pages=758–765|doi=10.1038/nchembio.121|pmid=18953358|issn=1552-4450|pmc=2587053}}</ref><ref name=":15">{{Cite journal|last1=Booker|first1=Squire J|last2=Cicchillo|first2=Robert M|last3=Grove|first3=Tyler L|date=October 2007|title=Self-sacrifice in radical S-adenosylmethionine proteins|journal=Current Opinion in Chemical Biology|volume=11|issue=5|pages=543–552|doi=10.1016/j.cbpa.2007.08.028|pmid=17936058|issn=1367-5931|pmc=2637762}}</ref> |
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He also researches many bacteria including ''[[Staphylococcus aureus]]'' which |
He also researches many bacteria including ''[[Staphylococcus aureus]]'', which is found in the nasal cavity and on the skin in humans.<ref name=":18">{{Cite journal|last1=Booker|first1=S.|last2=Stubbe|first2=J.|date=1993-09-15|title=Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.|journal=Proceedings of the National Academy of Sciences|volume=90|issue=18|pages=8352–8356|doi=10.1073/pnas.90.18.8352|pmid=8397403|pmc=47354|bibcode=1993PNAS...90.8352B|issn=0027-8424|doi-access=free}}</ref> ''S. aureus'' is problematic because it can mutate into the [[superbug]] [[Methicillin-resistant Staphylococcus aureus|methicillin-resistant ''S. aureus'' (MRSA)]].<ref>{{Cite journal|last=Sanders|first=Laura|date=2010-09-28|title=Genes & cells: Superbug secret revealed|journal=Science News|volume=178|issue=7|pages=9|doi=10.1002/scin.5591780708|issn=0036-8423}}</ref> There is a protein called Cfr protein in ''S. aureus'' that binds to ribosomes which is where translation occurs. Many antibiotics bind to ribosomes which cause bacteria to die. However, when Cfr is expressed, it binds to the ribosome and allows the bacteria to stay alive which is known as methylation<ref>{{Cite journal |last=Peng Jiang|first=Peng Jiang|date=2015-02-10|title=Sequencing the Cactus Genome to Discover the Secret of Drought Resistance |website=Experiment |url=https://experiment.com/projects/sequencing-the-cactus-genome-to-discover-the-secret-of-drought-resistance |doi=10.18258/4612}}</ref><ref>{{Cite journal|date=2011-09-28|title=Effective antibiotics are in sight after scientists unlock secrets of superbug|journal=Nursing Standard|volume=26|issue=4|pages=17|doi=10.7748/ns.26.4.17.s23|issn=0029-6570}}</ref><ref name=":19">{{Cite journal|last1=Bauerle|first1=Matthew R.|last2=Schwalm|first2=Erica L.|last3=Booker|first3=Squire J.|date=2014-12-04|title=Mechanistic Diversity of RadicalS-Adenosylmethionine (SAM)-dependent Methylation|journal=Journal of Biological Chemistry|volume=290|issue=7|pages=3995–4002|doi=10.1074/jbc.r114.607044|pmid=25477520|pmc=4326810|issn=0021-9258|doi-access=free}}</ref> |
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This research has led Booker to discover that ''S. aureus'' expresses a protein, Cfr, which makes it resistant to many [[antibiotic]]s.<ref name=":20">{{Cite journal|last1=Grove|first1=Tyler L|last2=Livada|first2=Jovan|last3=Schwalm|first3=Erica L|last4=Green|first4=Michael T|last5=Booker|first5=Squire J|last6=Silakov|first6=Alexey|date=2013-05-05|title=A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr|journal=Nature Chemical Biology|volume=9|issue=7|pages=422–427|doi=10.1038/nchembio.1251|pmid=23644479|issn=1552-4450|pmc=3897224}}</ref> He developed mechanism of this methylation.<ref name=":21">{{Cite journal|last1=Boal|first1=A. K.|last2=Grove|first2=T. L.|last3=McLaughlin|first3=M. I.|last4=Yennawar|first4=N. H.|last5=Booker|first5=S. J.|last6=Rosenzweig|first6=A. C.|date=2011-04-28|title=Structural Basis for Methyl Transfer by a Radical SAM Enzyme|journal=Science|volume=332|issue=6033|pages=1089–1092|doi=10.1126/science.1205358|pmid=21527678|issn=0036-8075|pmc=3506250|bibcode=2011Sci...332.1089B}}</ref><ref name=":22">{{Cite journal|last1=Grove|first1=T. L.|last2=Benner|first2=J. S.|last3=Radle|first3=M. I.|last4=Ahlum|first4=J. H.|last5=Landgraf|first5=B. J.|last6=Krebs|first6=C.|last7=Booker|first7=S. J.|s2cid=2214309|date=2011-03-17|title=A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases|journal=Science|volume=332|issue=6029|pages=604–607|doi=10.1126/science.1200877|pmid=21415317|bibcode=2011Sci...332..604G|issn=0036-8075}}</ref> Booker's lab also researches aspects of the bacterium, ''[[Escherichia coli]]''.<ref name=":24">{{Cite journal|last1=Lanz|first1=Nicholas D.|last2=Blaszczyk|first2=Anthony J.|last3=McCarthy|first3=Erin L.|last4=Wang|first4=Bo|last5=Wang|first5=Roy X.|last6=Jones|first6=Brianne S.|last7=Booker|first7=Squire J.|date=2018-01-03|title=Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in ''Escherichia coli''|journal=Biochemistry|volume=57|issue=9|pages=1475–1490|doi=10.1021/acs.biochem.7b01205|pmid=29298049|issn=0006-2960|pmc=5941297}}</ref><ref name=":25">{{Citation|last1=McCarthy|first1=Erin L.|title=Biochemical Approaches for Understanding Iron–Sulfur Cluster Regeneration in ''Escherichia coli'' Lipoyl Synthase During Catalysis|date=2018|journal=Methods in Enzymology|pages=217–239|publisher=Elsevier|isbn=978-0-12-812794-0|last2=Booker|first2=Squire J.|volume=606|doi=10.1016/bs.mie.2018.06.006|pmid=30097094|pmc=6501195}}</ref><ref name=":26">{{Cite journal|last1=Cicchillo|first1=Robert M.|last2=Lee|first2=Kyung-Hoon|last3=Baleanu-Gogonea|first3=Camelia|last4=Nesbitt|first4=Natasha M.|last5=Krebs|first5=Carsten|last6=Booker|first6=Squire J.|date=September 2004|title=''Escherichia coli'' Lipoyl Synthase Binds Two Distinct [4Fe−4S] Clusters per Polypeptide†|journal=Biochemistry|volume=43|issue=37|pages=11770–11781|doi=10.1021/bi0488505|pmid=15362861|issn=0006-2960}}</ref> He determined the three-dimensional structure of the RImN protein from the bacteria. RImN is one of two proteins which makes chemical modification to different RNA molecules. Understanding this structure will help with other research of [[Antimicrobial resistance|antibiotic resistance]].<ref>{{Cite journal|last=Pennisi|first=E.|date=1993-05-22|title=Cancer Cells Caught in the (Metastatic) Act|journal=Science News|volume=143|issue=21|pages=324|doi=10.2307/3977284|jstor=3977284|issn=0036-8423}}</ref><ref name=":27">{{Cite journal|last1=McCarthy|first1=Erin L.|last2=Rankin|first2=Ananda N.|last3=Dill|first3=Zerick R.|last4=Booker|first4=Squire J.|date=2018-12-11|title=The A-type domain in ''Escherichia coli'' NfuA is required for regenerating the auxiliary [4Fe–4S] cluster in ''Escherichia coli'' lipoyl synthase|journal=Journal of Biological Chemistry|volume=294|issue=5|pages=1609–1617|doi=10.1074/jbc.ra118.006171|pmid=30538130|pmc=6364782|issn=0021-9258|doi-access=free}}</ref> As a result of his research, he is synthesizing new compounds to stop the bacteria's defenses which would make antibiotics more effective.<ref name=":1" /><ref name="ARNAUD 13">{{Cite journal|last=ARNAUD|first=CELIA|title=Novel Antibiotic Mechanism|date=2007-08-13|journal=Chemical & Engineering News|volume=85|issue=33|pages=13|doi=10.1021/cen-v085n033.p013a|issn=0009-2347}}</ref> The goal of his research to design compounds which can prevent infections due to drug-resistant bacteria.<ref name="ARNAUD 13"/><ref name=":23">{{Cite journal|last1=Rajakovich|first1=Lauren J.|last2=Nørgaard|first2=Hanne|last3=Warui|first3=Douglas M.|last4=Chang|first4=Wei-chen|last5=Li|first5=Ning|last6=Booker|first6=Squire J.|last7=Krebs|first7=Carsten|last8=Bollinger|first8=J. Martin|last9=Pandelia|first9=Maria-Eirini|date=2015-09-02|title=Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism|journal=Journal of the American Chemical Society|volume=137|issue=36|pages=11695–11709|doi=10.1021/jacs.5b06345|pmid=26284355|issn=0002-7863}}</ref> |
This research has led Booker to discover that ''S. aureus'' expresses a protein, Cfr, which makes it resistant to many [[antibiotic]]s.<ref name=":20">{{Cite journal|last1=Grove|first1=Tyler L|last2=Livada|first2=Jovan|last3=Schwalm|first3=Erica L|last4=Green|first4=Michael T|last5=Booker|first5=Squire J|last6=Silakov|first6=Alexey|date=2013-05-05|title=A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr|journal=Nature Chemical Biology|volume=9|issue=7|pages=422–427|doi=10.1038/nchembio.1251|pmid=23644479|issn=1552-4450|pmc=3897224}}</ref> He developed mechanism of this methylation.<ref name=":21">{{Cite journal|last1=Boal|first1=A. K.|last2=Grove|first2=T. L.|last3=McLaughlin|first3=M. I.|last4=Yennawar|first4=N. H.|last5=Booker|first5=S. J.|last6=Rosenzweig|first6=A. C.|date=2011-04-28|title=Structural Basis for Methyl Transfer by a Radical SAM Enzyme|journal=Science|volume=332|issue=6033|pages=1089–1092|doi=10.1126/science.1205358|pmid=21527678|issn=0036-8075|pmc=3506250|bibcode=2011Sci...332.1089B}}</ref><ref name=":22">{{Cite journal|last1=Grove|first1=T. L.|last2=Benner|first2=J. S.|last3=Radle|first3=M. I.|last4=Ahlum|first4=J. H.|last5=Landgraf|first5=B. J.|last6=Krebs|first6=C.|last7=Booker|first7=S. J.|s2cid=2214309|date=2011-03-17|title=A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases|journal=Science|volume=332|issue=6029|pages=604–607|doi=10.1126/science.1200877|pmid=21415317|bibcode=2011Sci...332..604G|issn=0036-8075}}</ref> Booker's lab also researches aspects of the bacterium, ''[[Escherichia coli]]''.<ref name=":24">{{Cite journal|last1=Lanz|first1=Nicholas D.|last2=Blaszczyk|first2=Anthony J.|last3=McCarthy|first3=Erin L.|last4=Wang|first4=Bo|last5=Wang|first5=Roy X.|last6=Jones|first6=Brianne S.|last7=Booker|first7=Squire J.|date=2018-01-03|title=Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in ''Escherichia coli''|journal=Biochemistry|volume=57|issue=9|pages=1475–1490|doi=10.1021/acs.biochem.7b01205|pmid=29298049|issn=0006-2960|pmc=5941297}}</ref><ref name=":25">{{Citation|last1=McCarthy|first1=Erin L.|title=Biochemical Approaches for Understanding Iron–Sulfur Cluster Regeneration in ''Escherichia coli'' Lipoyl Synthase During Catalysis|date=2018|journal=Methods in Enzymology|pages=217–239|publisher=Elsevier|isbn=978-0-12-812794-0|last2=Booker|first2=Squire J.|volume=606|doi=10.1016/bs.mie.2018.06.006|pmid=30097094|pmc=6501195}}</ref><ref name=":26">{{Cite journal|last1=Cicchillo|first1=Robert M.|last2=Lee|first2=Kyung-Hoon|last3=Baleanu-Gogonea|first3=Camelia|last4=Nesbitt|first4=Natasha M.|last5=Krebs|first5=Carsten|last6=Booker|first6=Squire J.|date=September 2004|title=''Escherichia coli'' Lipoyl Synthase Binds Two Distinct [4Fe−4S] Clusters per Polypeptide†|journal=Biochemistry|volume=43|issue=37|pages=11770–11781|doi=10.1021/bi0488505|pmid=15362861|issn=0006-2960}}</ref> He determined the three-dimensional structure of the RImN protein from the bacteria. RImN is one of two proteins which makes chemical modification to different RNA molecules. Understanding this structure will help with other research of [[Antimicrobial resistance|antibiotic resistance]].<ref>{{Cite journal|last=Pennisi|first=E.|date=1993-05-22|title=Cancer Cells Caught in the (Metastatic) Act|journal=Science News|volume=143|issue=21|pages=324|doi=10.2307/3977284|jstor=3977284|issn=0036-8423}}</ref><ref name=":27">{{Cite journal|last1=McCarthy|first1=Erin L.|last2=Rankin|first2=Ananda N.|last3=Dill|first3=Zerick R.|last4=Booker|first4=Squire J.|date=2018-12-11|title=The A-type domain in ''Escherichia coli'' NfuA is required for regenerating the auxiliary [4Fe–4S] cluster in ''Escherichia coli'' lipoyl synthase|journal=Journal of Biological Chemistry|volume=294|issue=5|pages=1609–1617|doi=10.1074/jbc.ra118.006171|pmid=30538130|pmc=6364782|issn=0021-9258|doi-access=free}}</ref> As a result of his research, he is synthesizing new compounds to stop the bacteria's defenses which would make antibiotics more effective.<ref name=":1" /><ref name="ARNAUD 13">{{Cite journal|last=ARNAUD|first=CELIA|title=Novel Antibiotic Mechanism|date=2007-08-13|journal=Chemical & Engineering News|volume=85|issue=33|pages=13|doi=10.1021/cen-v085n033.p013a|issn=0009-2347}}</ref> The goal of his research to design compounds which can prevent infections due to drug-resistant bacteria.<ref name="ARNAUD 13"/><ref name=":23">{{Cite journal|last1=Rajakovich|first1=Lauren J.|last2=Nørgaard|first2=Hanne|last3=Warui|first3=Douglas M.|last4=Chang|first4=Wei-chen|last5=Li|first5=Ning|last6=Booker|first6=Squire J.|last7=Krebs|first7=Carsten|last8=Bollinger|first8=J. Martin|last9=Pandelia|first9=Maria-Eirini|date=2015-09-02|title=Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism|journal=Journal of the American Chemical Society|volume=137|issue=36|pages=11695–11709|doi=10.1021/jacs.5b06345|pmid=26284355|issn=0002-7863}}</ref> |
Revision as of 11:38, 15 April 2022
Squire Booker is an American biochemist at Penn State University.[1] Booker directs an interdisciplinary chemistry research program related to fields of biochemistry, enzymology, protein chemistry, natural product biosynthesis, and mechanisms of radical dependent enzymes.[1][2] He is an associate editor for the American Chemical Society Biochemistry Journal,[2] is a Hughes Medical Institute Investigator,[1][2][3] and an Eberly Distinguished Chair in Science at Penn State University.[1][4]
Early life
Booker was born September 9, 1965. He grew up in the segregated community of Beaumont, Texas. He was raised by his grandmother with the help of three uncles.[5][6][7]
Education
Booker received his B.A. in chemistry at Austin College in 1987,[1] where he was a Minnie Stevens Piper Scholar.[8] He received his Ph.D. in biochemistry from Massachusetts Institute of Technology in 1994,[1] and conducted postdoctoral research at Universite Rene Decartes in Paris, France and held a Postdoctoral Fellowship at the Institute for Enzyme Research at the University of Wisconsin. He became a professor at Penn State University in 1999,[9] where he earned tenure in 2005.[10]
Research
Booker is a professor of biology, biochemistry, and molecular biology at Penn State University.[1][2] His research explores how enzymes change their catalytic abilities due to metal ions or metal clusters.[11][12] His research focuses on enzymes containing iron-sulfur clusters which catalyze chemical reactions.[1][13][14] He focuses on the Radical S-adenosylamethionine Superfamily (SAM) which is a group of enzymes that encounters radical chemistry in post-transcriptional and post-translational modifications of DNA.[1][15][16][17]
He also researches many bacteria including Staphylococcus aureus, which is found in the nasal cavity and on the skin in humans.[18] S. aureus is problematic because it can mutate into the superbug methicillin-resistant S. aureus (MRSA).[19] There is a protein called Cfr protein in S. aureus that binds to ribosomes which is where translation occurs. Many antibiotics bind to ribosomes which cause bacteria to die. However, when Cfr is expressed, it binds to the ribosome and allows the bacteria to stay alive which is known as methylation[20][21][22]
This research has led Booker to discover that S. aureus expresses a protein, Cfr, which makes it resistant to many antibiotics.[23] He developed mechanism of this methylation.[24][25] Booker's lab also researches aspects of the bacterium, Escherichia coli.[26][27][28] He determined the three-dimensional structure of the RImN protein from the bacteria. RImN is one of two proteins which makes chemical modification to different RNA molecules. Understanding this structure will help with other research of antibiotic resistance.[29][30] As a result of his research, he is synthesizing new compounds to stop the bacteria's defenses which would make antibiotics more effective.[2][31] The goal of his research to design compounds which can prevent infections due to drug-resistant bacteria.[31][32]
Activism
Booker is active in promoting diversity in Science, Technology, Engineering, and Mathematics (STEM) especially towards undergraduate and graduate students. He was a chair on the Minority Affairs Committee of the American Association of Biochemistry and Molecular Biology.[8] In 2010, he helped organize a workshop which discussed the different obstacles and challenges that minorities in biochemistry and molecular biology encounter when building externally funded research programs.[33][34]
Booker was the guest speaker at Massachusetts Institute of Technology's 2019 Investiture of Doctoral Hoods and Degree Conferral Ceremony.[6] He was chosen due to his impressive contributions to the scientific community and his activism towards inclusion of all in STEM. In his speech, he emphasized an opportunity for all in science.[5] He encouraged the graduates to take responsibility and give back to society. It does not matter what one's background is in, people in STEM need to be willing to accept and stand up for each other.[7][6]
Honors and awards
Booker has received numerous honor and awards:
- 2019 Associate Editor for the American Chemical Society Biochemistry Journal[2]
- 2018 Evan Pugh Professor at Penn State University[35][8]
- 2017 Eberly Distinguished Chair in Science at Penn State University[1][4]
- 2017 Elected to the American Academy of Arts and Sciences[1][9]
- 2017 Lloyd N. Ferguson Distinguished Lecturer at Cal State, Los Angeles[1]
- 2016 Penn State Faculty Scholar Medal[1][9][4]
- 2016 Scott Lectureship in Chemistry and Biochemistry at the University of Florida[1]
- 2016 Co-organizer of the ASBMB Annual Meeting[1][33][34]
- 2015 Selected as a Hughes Medical Investigator[1][2][3][8][9]
- 2015 Everson Lectureship in Biochemistry at the University of Wisconsin, Madison[1]
- 2014 Fellow of the American Association for the Advancement of Science[8][36]
- 2013 TY Shen Lectureship in Biological Chemistry at MIT[1]
- 2011 American Chemical Society Arthur C. Cope Scholar Award[1][8]
- 2006 co-chair, GRC on Enzyme Coenzymes and Metabolic Pathways[1]
- 2004 Presidential Early Career Award in Science and Engineering[1][8]
- 2002-2007 NSF Faculty Early Career Award[1][4]
- 1996-1999 NIH Postdoctoral Fellow at the Institute for Enzyme Research at the University of Wisconsin[1][8][9]
- 1994-1995 NSF-NATO Postdoctoral Fellow[1][8][9]
Selected publications
Booker has published over 100 scientific publications in journals such as the Journal of the American Chemical Society and Proceedings of the National Academy of Sciences.[8] Here are some of the most cited publications:
- Grove, T. L.; Benner, J. S.; Radle, M. I.; Ahlum, J. H.; Landgraf, B. J.; Krebs, C.; Booker, S. J. (2011). "A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases". Science. 332 (6029): 604–607. Bibcode:2011Sci...332..604G. doi:10.1126/science.1200877. PMID 21415317. S2CID 2214309.
- Matthews, M. L.; Neumann, C. S.; Miles, L. A.; Grove, T. L.; Booker, S. J.; Krebs, C.; Walsh, C. T.; Bollinger, J. M. (2009). "Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2". Proceedings of the National Academy of Sciences. 106 (42): 17723–17728. Bibcode:2009PNAS..10617723M. doi:10.1073/pnas.0909649106. PMC 2764930. PMID 19815524.
- Boal, A. K.; Grove, T. L.; McLaughlin, M. I.; Yennawar, N. H.; Booker, S. J.; Rosenzweig, A. C. (2011). "Structural Basis for Methyl Transfer by a Radical SAM Enzyme". Science. 332 (6033): 1089–1092. Bibcode:2011Sci...332.1089B. doi:10.1126/science.1205358. PMC 3506250. PMID 21527678.
References
- ^ a b c d e f g h i j k l m n o p q r s t u v w x "Squire J. Booker — Penn State University - Department of Chemistry". chem.psu.edu. Retrieved 2020-01-26.
- ^ a b c d e f g Schepartz, Alanna (2019-12-24). "Welcome New Associate Editor, Squire Booker". Biochemistry. 58 (51): 5099. doi:10.1021/acs.biochem.9b01057. ISSN 0006-2960. PMID 31870158.
- ^ a b "Keston News Service, No.301, May 26, 1988, 22 pp". Human Rights Documents Online. doi:10.1163/2210-7975_hrd-0328-0272.
- ^ a b c d Stokley, James (1931-02-07). "February Evening Skies". The Science News-Letter. 19 (513): 85–86. doi:10.2307/3906900. ISSN 0096-4018. JSTOR 3906900.
- ^ a b "Central States to Provide Employment Service". Anthropology News. 18 (1): 5. January 1977. doi:10.1111/an.1977.18.1.5.2. ISSN 1541-6151.
- ^ a b c DiGirolamo, Vincent (2019-09-19), "Call to Service", Crying the News: A History of America's Newsboys, Oxford University Press, pp. 441–472, doi:10.1093/oso/9780195320251.003.0013, ISBN 978-0-19-532025-1
- ^ a b Indonesia Economic Quarterly, June 2019 (PDF). World Bank. June 2019. doi:10.1596/31993.
- ^ a b c d e f g h i j "Better/Service for AMERICA'S LABORATORIES IN THE Central States". Chemical & Engineering News. 22 (11): 878. 1944-06-10. doi:10.1021/cen-v022n011.p878. ISSN 0009-2347.
- ^ a b c d e f "Anthropologists Elected to NAS and American Academy of Arts and Sciences". Anthropology News. 21 (6): 14. September 1980. doi:10.1111/an.1980.21.6.14.2. ISSN 1541-6151.
- ^ "Biochemistry in the Age of Big Data".
{{cite web}}
: CS1 maint: url-status (link) - ^ Elango, B. (2015), "United States Service Sector Data", Service Industry Databook, Springer International Publishing, pp. 17–55, doi:10.1007/978-3-319-19111-9_3, ISBN 978-3-319-19110-2
- ^ Cicchillo, Robert M.; Iwig, David F.; Jones, A. Daniel; Nesbitt, Natasha M.; Baleanu-Gogonea, Camelia; Souder, Matthew G.; Tu, Loretta; Booker, Squire J. (June 2004). "Lipoyl Synthase Requires Two Equivalents ofS-Adenosyl-l-methionine To Synthesize One Equivalent of Lipoic Acid†". Biochemistry. 43 (21): 6378–6386. doi:10.1021/bi049528x. ISSN 0006-2960. PMID 15157071.
- ^ Lieder, Kafryn W.; Booker, Squire; Ruzicka, Frank J.; Beinert, Helmut; Reed, George H.; Frey, Perry A. (February 1998). "S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron−Sulfur Centers by Electron Paramagnetic Resonance†". Biochemistry. 37 (8): 2578–2585. doi:10.1021/bi972417w. ISSN 0006-2960. PMID 9485408.
- ^ Blaszczyk, Anthony J.; Silakov, Alexey; Zhang, Bo; Maiocco, Stephanie J.; Lanz, Nicholas D.; Kelly, Wendy L.; Elliott, Sean J.; Krebs, Carsten; Booker, Squire J. (2016-03-03). "Spectroscopic and Electrochemical Characterization of the Iron–Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase". Journal of the American Chemical Society. 138 (10): 3416–3426. doi:10.1021/jacs.5b12592. ISSN 0002-7863. PMID 26841310.
- ^ Grove, Tyler L.; Lee, Kyung-Hoon; St. Clair, Jennifer; Krebs, Carsten; Booker, Squire J. (July 2008). "In Vitro Characterization of AtsB, a Radical SAM Formylglycine-Generating Enzyme That Contains Three [4Fe-4S] Clusters†". Biochemistry. 47 (28): 7523–7538. doi:10.1021/bi8004297. ISSN 0006-2960. PMC 2664749. PMID 18558715.
- ^ Chatterjee, Abhishek; Li, Yue; Zhang, Yang; Grove, Tyler L; Lee, Michael; Krebs, Carsten; Booker, Squire J; Begley, Tadhg P; Ealick, Steven E (2008-10-26). "Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily". Nature Chemical Biology. 4 (12): 758–765. doi:10.1038/nchembio.121. ISSN 1552-4450. PMC 2587053. PMID 18953358.
- ^ Booker, Squire J; Cicchillo, Robert M; Grove, Tyler L (October 2007). "Self-sacrifice in radical S-adenosylmethionine proteins". Current Opinion in Chemical Biology. 11 (5): 543–552. doi:10.1016/j.cbpa.2007.08.028. ISSN 1367-5931. PMC 2637762. PMID 17936058.
- ^ Booker, S.; Stubbe, J. (1993-09-15). "Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii". Proceedings of the National Academy of Sciences. 90 (18): 8352–8356. Bibcode:1993PNAS...90.8352B. doi:10.1073/pnas.90.18.8352. ISSN 0027-8424. PMC 47354. PMID 8397403.
- ^ Sanders, Laura (2010-09-28). "Genes & cells: Superbug secret revealed". Science News. 178 (7): 9. doi:10.1002/scin.5591780708. ISSN 0036-8423.
- ^ Peng Jiang, Peng Jiang (2015-02-10). "Sequencing the Cactus Genome to Discover the Secret of Drought Resistance". Experiment. doi:10.18258/4612.
- ^ "Effective antibiotics are in sight after scientists unlock secrets of superbug". Nursing Standard. 26 (4): 17. 2011-09-28. doi:10.7748/ns.26.4.17.s23. ISSN 0029-6570.
- ^ Bauerle, Matthew R.; Schwalm, Erica L.; Booker, Squire J. (2014-12-04). "Mechanistic Diversity of RadicalS-Adenosylmethionine (SAM)-dependent Methylation". Journal of Biological Chemistry. 290 (7): 3995–4002. doi:10.1074/jbc.r114.607044. ISSN 0021-9258. PMC 4326810. PMID 25477520.
- ^ Grove, Tyler L; Livada, Jovan; Schwalm, Erica L; Green, Michael T; Booker, Squire J; Silakov, Alexey (2013-05-05). "A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr". Nature Chemical Biology. 9 (7): 422–427. doi:10.1038/nchembio.1251. ISSN 1552-4450. PMC 3897224. PMID 23644479.
- ^ Boal, A. K.; Grove, T. L.; McLaughlin, M. I.; Yennawar, N. H.; Booker, S. J.; Rosenzweig, A. C. (2011-04-28). "Structural Basis for Methyl Transfer by a Radical SAM Enzyme". Science. 332 (6033): 1089–1092. Bibcode:2011Sci...332.1089B. doi:10.1126/science.1205358. ISSN 0036-8075. PMC 3506250. PMID 21527678.
- ^ Grove, T. L.; Benner, J. S.; Radle, M. I.; Ahlum, J. H.; Landgraf, B. J.; Krebs, C.; Booker, S. J. (2011-03-17). "A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases". Science. 332 (6029): 604–607. Bibcode:2011Sci...332..604G. doi:10.1126/science.1200877. ISSN 0036-8075. PMID 21415317. S2CID 2214309.
- ^ Lanz, Nicholas D.; Blaszczyk, Anthony J.; McCarthy, Erin L.; Wang, Bo; Wang, Roy X.; Jones, Brianne S.; Booker, Squire J. (2018-01-03). "Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in Escherichia coli". Biochemistry. 57 (9): 1475–1490. doi:10.1021/acs.biochem.7b01205. ISSN 0006-2960. PMC 5941297. PMID 29298049.
- ^ McCarthy, Erin L.; Booker, Squire J. (2018), "Biochemical Approaches for Understanding Iron–Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis", Methods in Enzymology, 606, Elsevier: 217–239, doi:10.1016/bs.mie.2018.06.006, ISBN 978-0-12-812794-0, PMC 6501195, PMID 30097094
- ^ Cicchillo, Robert M.; Lee, Kyung-Hoon; Baleanu-Gogonea, Camelia; Nesbitt, Natasha M.; Krebs, Carsten; Booker, Squire J. (September 2004). "Escherichia coli Lipoyl Synthase Binds Two Distinct [4Fe−4S] Clusters per Polypeptide†". Biochemistry. 43 (37): 11770–11781. doi:10.1021/bi0488505. ISSN 0006-2960. PMID 15362861.
- ^ Pennisi, E. (1993-05-22). "Cancer Cells Caught in the (Metastatic) Act". Science News. 143 (21): 324. doi:10.2307/3977284. ISSN 0036-8423. JSTOR 3977284.
- ^ McCarthy, Erin L.; Rankin, Ananda N.; Dill, Zerick R.; Booker, Squire J. (2018-12-11). "The A-type domain in Escherichia coli NfuA is required for regenerating the auxiliary [4Fe–4S] cluster in Escherichia coli lipoyl synthase". Journal of Biological Chemistry. 294 (5): 1609–1617. doi:10.1074/jbc.ra118.006171. ISSN 0021-9258. PMC 6364782. PMID 30538130.
- ^ a b ARNAUD, CELIA (2007-08-13). "Novel Antibiotic Mechanism". Chemical & Engineering News. 85 (33): 13. doi:10.1021/cen-v085n033.p013a. ISSN 0009-2347.
- ^ Rajakovich, Lauren J.; Nørgaard, Hanne; Warui, Douglas M.; Chang, Wei-chen; Li, Ning; Booker, Squire J.; Krebs, Carsten; Bollinger, J. Martin; Pandelia, Maria-Eirini (2015-09-02). "Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism". Journal of the American Chemical Society. 137 (36): 11695–11709. doi:10.1021/jacs.5b06345. ISSN 0002-7863. PMID 26284355.
- ^ a b "NSF Outreach Service". Anthropology News. 26 (4): 13. April 1985. doi:10.1111/an.1985.26.4.13.4. ISSN 1541-6151.
- ^ a b "News briefing: 30 July–5 August 2010". Nature. 466 (7307): 670–671. August 2010. doi:10.1038/466670a. ISSN 0028-0836.
- ^ "ACS News". Chemical & Engineering News. 56 (25): 38–39. 1978-06-19. doi:10.1021/cen-v056n025.p038. ISSN 0009-2347.
- ^ "Psychologist Steven Breckler named fellow of American Association for the Advancement of Science" (Document). 2008. doi:10.1037/e539992008-001.
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- Living people
- Pennsylvania State University faculty
- American biochemists
- African-American chemists
- Fellows of the American Association for the Advancement of Science
- Austin College alumni
- Massachusetts Institute of Technology School of Science alumni
- Members of the United States National Academy of Sciences
- 1965 births
- 21st-century African-American people
- 20th-century African-American people