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'''Dino Moras''', born on 23 November 1944, is a French [[biochemist]], research director at the [[Centre national de la recherche scientifique|CNRS]] and co-director of the Institute of Genetics and Molecular and Cellular Biology (IGBMC)<ref>{{cite web|title=Équipe Biologie structurale intégrative|url=http://www.igbmc.fr/research/department/3/team/37/|agency=[[Institut de génétique et de biologie moléculaire et cellulaire]]|access-date=12 April 2019|publication-date=}}</ref> in [[Illkirch-Graffenstaden]] until 2010<ref name="CV">[http://www.academie-sciences.fr/academie/membre/MorasD_bio0511.pdf Académie des sciences : Dino Moras], [[Curriculum vitæ|CV]] sur le site de l'[[Académie des sciences (France)|Académie des sciences]] : www.academie-sciences.fr. Accessed 14 Feb 2013</ref>
'''Dino Moras''', born on 23 November 1944, is a French [[biochemist]], research director at the [[Centre national de la recherche scientifique|CNRS]] and co-director of the Institute of Genetics and Molecular and Cellular Biology (IGBMC)<ref>{{cite web|title=Équipe Biologie structurale intégrative|url=http://www.igbmc.fr/research/department/3/team/37/|agency=[[Institut de génétique et de biologie moléculaire et cellulaire]]|access-date=12 April 2019|date=}}</ref> in [[Illkirch-Graffenstaden]] until 2010<ref name="CV">[http://www.academie-sciences.fr/academie/membre/MorasD_bio0511.pdf Académie des sciences : Dino Moras], [[Curriculum vitæ|CV]] sur le site de l'[[Académie des sciences (France)|Académie des sciences]] : www.academie-sciences.fr. Accessed 14 Feb 2013</ref>


== Biography ==
== Biography ==


Dino Moras is a [[chemist]] by training with a [[thesis]] defended in 1971 at the [[University of Strasbourg]], formerly Louis-Pasteur University. After a [[post-doctoral fellowship]] at [[Purdue University]] in [[Indiana]], [[United States|USA]], he joined the CNRS in the mid-1970s and worked with [[Pierre Chambon]]. He became a member of the [[American Academy of Arts and Sciences]] in 1998 and a full member of the [[Academy of sciences|Academy of Sciences]] in 1999<ref>{{cite web|title=Présentation de Dino Moras|url=http://www.academie-sciences.fr/academie/membre/Moras_Dino.htm|author=[[Académie des sciences (France)|Académie des sciences]]|website=www.academie-sciences.fr|language=fr|access-date=18 February 2014|publication-date=}}</ref>.
Dino Moras is a [[chemist]] by training with a [[thesis]] defended in 1971 at the [[University of Strasbourg]], formerly Louis-Pasteur University. After a [[post-doctoral fellowship]] at [[Purdue University]] in [[Indiana]], [[United States|USA]], he joined the CNRS in the mid-1970s and worked with [[Pierre Chambon]]. He became a member of the [[American Academy of Arts and Sciences]] in 1998 and a full member of the [[Academy of sciences|Academy of Sciences]] in 1999<ref>{{cite web|title=Présentation de Dino Moras|url=http://www.academie-sciences.fr/academie/membre/Moras_Dino.htm|author=Académie des sciences|website=www.academie-sciences.fr|language=fr|access-date=18 February 2014|date=|author-link=Académie des sciences (France)}}</ref>.


In 2002, following Pierre Chambon and [[Jean-Louis Mandel]], he was Deputy Director and then Director of the IGBMC in Strasbourg from 2002 to 2010.
In 2002, following Pierre Chambon and [[Jean-Louis Mandel]], he was Deputy Director and then Director of the IGBMC in Strasbourg from 2002 to 2010.
Line 11: Line 11:
=== Chemistry ===
=== Chemistry ===


1968 - Synthesis and structure determination of a [[heterocycle]] without [[carbon atom]]<ref>{{Cite journal|last=Moras, D.|first=|date=1968|title=Crystal structure of di-(phosporyl trichloride) hexachloroditin (IV) di- u dichlorophosphate|url=|journal=Chem. Comm.|volume=26|pages=|via=}}</ref>.
1968 - Synthesis and structure determination of a [[heterocycle]] without [[carbon atom]]<ref>{{Cite journal|last=Moras, D.|date=1968|title=Crystal structure of di-(phosporyl trichloride) hexachloroditin (IV) di- u dichlorophosphate|url=|journal=Chem. Comm.|volume=26|pages=|via=}}</ref>.


1971 - Structure determination of heterocyclic cryptates<ref>{{Cite journal|last=Metz, B.|first=|date=1970|title=Crystal structure of a rubidium "cryptate"|url=|journal=Chem. Comm.,|volume=217|pages=|via=}}</ref>.
1971 - Structure determination of heterocyclic cryptates<ref>{{Cite journal|last=Metz, B.|date=1970|title=Crystal structure of a rubidium "cryptate"|url=|journal=Chem. Comm.|volume=217|pages=|via=}}</ref>.


1982 - First structural characterization and imaging of H3O+, the [[Catalysis|catalytic]] intermediate at the heart of acid-base catalysis postulated by [[Johannes Nicolaus Brønsted|Brönsted]] in 1918)<ref>{{Cite journal|last=Behr, J.P.|first=|date=1982|title=The H30+cation: molecular structure of an oxonium-macrocyclic polyether complex|url=|journal=J. Amer. Chem. Soc.|volume=104|pages=4540-4543|via=}}</ref>.
1982 - First structural characterization and imaging of H3O+, the [[Catalysis|catalytic]] intermediate at the heart of acid-base catalysis postulated by [[Johannes Nicolaus Brønsted|Brönsted]] in 1918)<ref>{{Cite journal|last=Behr, J.P.|date=1982|title=The H30+cation: molecular structure of an oxonium-macrocyclic polyether complex|url=|journal=J. Amer. Chem. Soc.|volume=104|pages=4540–4543|doi=10.1021/ja00381a007}}</ref>.


=== Structural Biology ===
=== Structural Biology ===
Line 21: Line 21:
==== Structure-function relationships in transfer RNAs (tRNAs) and aminoacyl-tRNA synthetases and their relation to the origin of the genetic code ====
==== Structure-function relationships in transfer RNAs (tRNAs) and aminoacyl-tRNA synthetases and their relation to the origin of the genetic code ====


(i) Crystal structure of tRNAasp, the second to be solved at atomic resolution<ref>{{Cite journal|last=Moras D.|first=|date=1980|title=3D structure of yeast tRNAAsp|url=|journal=Nature|volume=288|pages=669-674|via=}}</ref>.
(i) Crystal structure of tRNAasp, the second to be solved at atomic resolution<ref>{{Cite journal|last=Moras D.|date=1980|title=3D structure of yeast tRNAAsp|url=|journal=Nature|volume=288|pages=669–674|doi=10.1038/288669a0}}</ref>.


(ii) Partition of aaRSs into two classes based on structural and functional correlation (each class of enzymes targets different chiral centers)<ref>{{Cite journal|last=Eriani, G.|first=|date=1990|title=Partition of tRNA-synthetases into two classes based on mutually exclusive sets of sequence motifs|url=|journal=Nature|volume=347|pages=203-206|via=}}</ref>.
(ii) Partition of aaRSs into two classes based on structural and functional correlation (each class of enzymes targets different chiral centers)<ref>{{Cite journal|last=Eriani, G.|date=1990|title=Partition of tRNA-synthetases into two classes based on mutually exclusive sets of sequence motifs|url=|journal=Nature|volume=347|issue=6289|pages=203–206|doi=10.1038/347203a0|bibcode=1990Natur.347..203E}}</ref>.


(iii) The first structure determination of a class II tRNA-aaRS complex<ref>{{Cite journal|last=Ruff, M.|first=|date=1991|title=Class II aminoacyl tRNA-synthetases : crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNAAsp.|url=|journal=Science|volume=252|pages=1682 - 1689|via=}}</ref> led to the elucidation of the reaction mechanism for the [[aspartic acid]] system, prototypic of all class II enzymes. It provided the structural explanation for the different [[chirality]] of the targets in the two classes. Further the crystal structure led to the discovery and functional characterization of a novel conformation of [[adenosine triphosphate]] (ATP)<ref>{{Cite journal|last=Cavarelli, J.|first=|date=1994|title=The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction|url=|journal=EMBO J.|volume=113(2)|pages=327-37|via=}}</ref>. The latter was so far only found in class II [[Enzyme|enzymes]].
(iii) The first structure determination of a class II tRNA-aaRS complex<ref>{{Cite journal|last=Ruff, M.|date=1991|title=Class II aminoacyl tRNA-synthetases : crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNAAsp.|url=|journal=Science|volume=252|pages=1682–1689|doi=10.1126/science.2047877}}</ref> led to the elucidation of the reaction mechanism for the [[aspartic acid]] system, prototypic of all class II enzymes. It provided the structural explanation for the different [[chirality]] of the targets in the two classes. Further the crystal structure led to the discovery and functional characterization of a novel conformation of [[adenosine triphosphate]] (ATP)<ref>{{Cite journal|last=Cavarelli, J.|date=1994|title=The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction|url=|journal=EMBO J.|volume=113|issue=2|pages=327–37|via=}}</ref>. The latter was so far only found in class II [[Enzyme|enzymes]].


(iv) The crystal structure of threonyl-tRNA synthetase enlightened the molecular mechanism of the editing reaction to correct for tRNA mischarging by serine thus solving the related Pauling paradox for the fidelity of translation<ref>{{Cite journal|last=Sankaranarayanan, R.|first=|date=1999|title=The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site|url=|journal=Cell|volume=97|pages=371-381|via=}}</ref><ref>{{Cite journal|last=Dock-Bregeon, A-C.|first=|date=2000|title=Transfer RNA-Mediated editing in threonyl-tRNA synthetase : The class II solution to the double discrimination problem|url=|journal=Cell|volume=103|pages=1-20|via=}}</ref>.
(iv) The crystal structure of threonyl-tRNA synthetase enlightened the molecular mechanism of the editing reaction to correct for tRNA mischarging by serine thus solving the related Pauling paradox for the fidelity of translation<ref>{{Cite journal|last=Sankaranarayanan, R.|date=1999|title=The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site|url=|journal=Cell|volume=97|issue=3|pages=371–381|doi=10.1016/S0092-8674(00)80746-1}}</ref><ref>{{Cite journal|last=Dock-Bregeon, A-C.|date=2000|title=Transfer RNA-Mediated editing in threonyl-tRNA synthetase : The class II solution to the double discrimination problem|url=|journal=Cell|volume=103|pages=1–20|via=}}</ref>.


==== Transcription regulation by Nuclear Hormones Receptors (NRs) ====
==== Transcription regulation by Nuclear Hormones Receptors (NRs) ====
Line 33: Line 33:
The superfamily of NRs, ligand-dependent [[Transcription factor|transcription factors]], regulates the expression of important target genes. NRs control most physiological functions and are implicated in several pathological processes.
The superfamily of NRs, ligand-dependent [[Transcription factor|transcription factors]], regulates the expression of important target genes. NRs control most physiological functions and are implicated in several pathological processes.
In 1995 he solved the first crystal structures of the ligand binding domains (LBDs) of two NRs of [[Retinoid|retinoids]] (RXR and RAR) in their apo and liganded form respectively<ref>{{Cite journal|last=Bourguet, W.|first=|date=1995|title=Crystal structure of the Ligand Binding Domain of the Human Nuclear Receptor RXRα|url=|journal=Nature|volume=375|pages=377-382|via=}}</ref><ref>{{Cite journal|last=Renaud, J.-P.|first=|date=1995|title=Crystal Structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid|url=|journal=Nature|volume=378|pages=681-689|via=}}</ref>. These structures allowed to define a canonical unique fold for the whole family and revealed the molecular mechanism of [[ligand]] dependent activation, setting up the bases for the design of [[agonist]] and [[antagonist]] drugs<ref>{{Cite journal|last=Brelivet, Y.|first=|date=2004|title=Signature of the oligomeric behavior of nuclear receptors at the sequence and structural level|url=|journal=EMBO Reports|volume=5|pages=423-429|via=}}</ref>. The crystal structure of RXR LBD was the first determination of a [[protein]] structure using [[Xenon]] as heavy atom derivative.
In 1995 he solved the first crystal structures of the ligand binding domains (LBDs) of two NRs of [[Retinoid|retinoids]] (RXR and RAR) in their apo and liganded form respectively<ref>{{Cite journal|last=Bourguet, W.|date=1995|title=Crystal structure of the Ligand Binding Domain of the Human Nuclear Receptor RXRα|url=|journal=Nature|volume=375|issue=6530|pages=377–382|doi=10.1038/375377a0|bibcode=1995Natur.375..377B}}</ref><ref>{{Cite journal|last=Renaud, J.-P.|date=1995|title=Crystal Structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid|url=|journal=Nature|volume=378|issue=6558|pages=681–689|doi=10.1038/378681a0|bibcode=1995Natur.378..681R}}</ref>. These structures allowed to define a canonical unique fold for the whole family and revealed the molecular mechanism of [[ligand]] dependent activation, setting up the bases for the design of [[agonist]] and [[antagonist]] drugs<ref>{{Cite journal|last=Brelivet, Y.|date=2004|title=Signature of the oligomeric behavior of nuclear receptors at the sequence and structural level|url=|journal=EMBO Reports|volume=5|issue=4|pages=423–429|doi=10.1038/sj.embor.7400119}}</ref>. The crystal structure of RXR LBD was the first determination of a [[protein]] structure using [[Xenon]] as heavy atom derivative.
His team contributed several other molecular structures of NRs LBDs, notably those of human VDR ([[vitamin D]]) and insect’s receptor Ecdysone (EcR)<ref>{{Cite journal|last=Rochel, N.|first=|date=2000|title=The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand|url=|journal=Mol Cell|volume=5|pages=173-179|via=}}</ref><ref>{{Cite journal|last=Billas, IM.|first=|date=2003|title=Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor|url=|journal=Nature|volume=426|pages=91-96|via=}}</ref>.
His team contributed several other molecular structures of NRs LBDs, notably those of human VDR ([[vitamin D]]) and insect’s receptor Ecdysone (EcR)<ref>{{Cite journal|last=Rochel, N.|date=2000|title=The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand|url=|journal=Mol Cell|volume=5|pages=173–179|doi=10.1016/S1097-2765(00)80413-X}}</ref><ref>{{Cite journal|last=Billas, IM.|date=2003|title=Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor|url=|journal=Nature|volume=426|issue=6962|pages=91–96|doi=10.1038/nature02112|bibcode=2003Natur.426...91B}}</ref>.


In 2004 a comparative analysis of the primary sequences lead to the partition of the superfamily into two classes according to mutually exclusive invariant aminoacids. A functional correlation with clear evolutionary implications could be made with their dimerization properties. Class I receptors encompasses homodimers or monomers while class II assembles the receptors that form heterodimers with RXR<ref>{{Cite journal|last=Rochel, N.|first=2011|date=|title=Common architecture Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacing|url=|journal=Nat Struct Mol Biol.|volume=18|pages=564-70|via=}}</ref>.
In 2004 a comparative analysis of the primary sequences lead to the partition of the superfamily into two classes according to mutually exclusive invariant aminoacids. A functional correlation with clear evolutionary implications could be made with their dimerization properties. Class I receptors encompasses homodimers or monomers while class II assembles the receptors that form heterodimers with RXR<ref>{{Cite journal|last=Rochel, N.|first=2011|date=|title=Common architecture Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacing|url=|journal=Nat Struct Mol Biol.|volume=18|pages=564–70|doi=10.1038/nsmb.2054}}</ref>.


In order to decipher the structural bases of the communication between nuclear receptors, DNA and components of the basal transcription machinery he used the multi-scale approach of integrative structural biology. The solution structures of several nuclear receptors heterodimers bound to their DNA response elements was the first milestone (16). It was followed by the cryo-EM structure determination of two additional complexes (17,18).
In order to decipher the structural bases of the communication between nuclear receptors, DNA and components of the basal transcription machinery he used the multi-scale approach of integrative structural biology. The solution structures of several nuclear receptors heterodimers bound to their DNA response elements was the first milestone (16). It was followed by the cryo-EM structure determination of two additional complexes (17,18).

Revision as of 21:37, 6 July 2019

Dino Moras, born on 23 November 1944, is a French biochemist, research director at the CNRS and co-director of the Institute of Genetics and Molecular and Cellular Biology (IGBMC)[1] in Illkirch-Graffenstaden until 2010[2]

Biography

Dino Moras is a chemist by training with a thesis defended in 1971 at the University of Strasbourg, formerly Louis-Pasteur University. After a post-doctoral fellowship at Purdue University in Indiana, USA, he joined the CNRS in the mid-1970s and worked with Pierre Chambon. He became a member of the American Academy of Arts and Sciences in 1998 and a full member of the Academy of Sciences in 1999[3].

In 2002, following Pierre Chambon and Jean-Louis Mandel, he was Deputy Director and then Director of the IGBMC in Strasbourg from 2002 to 2010.

Main Scientific contributions

Chemistry

1968 - Synthesis and structure determination of a heterocycle without carbon atom[4].

1971 - Structure determination of heterocyclic cryptates[5].

1982 - First structural characterization and imaging of H3O+, the catalytic intermediate at the heart of acid-base catalysis postulated by Brönsted in 1918)[6].

Structural Biology

Structure-function relationships in transfer RNAs (tRNAs) and aminoacyl-tRNA synthetases and their relation to the origin of the genetic code

(i) Crystal structure of tRNAasp, the second to be solved at atomic resolution[7].

(ii) Partition of aaRSs into two classes based on structural and functional correlation (each class of enzymes targets different chiral centers)[8].

(iii) The first structure determination of a class II tRNA-aaRS complex[9] led to the elucidation of the reaction mechanism for the aspartic acid system, prototypic of all class II enzymes. It provided the structural explanation for the different chirality of the targets in the two classes. Further the crystal structure led to the discovery and functional characterization of a novel conformation of adenosine triphosphate (ATP)[10]. The latter was so far only found in class II enzymes.

(iv) The crystal structure of threonyl-tRNA synthetase enlightened the molecular mechanism of the editing reaction to correct for tRNA mischarging by serine thus solving the related Pauling paradox for the fidelity of translation[11][12].

Transcription regulation by Nuclear Hormones Receptors (NRs)

The superfamily of NRs, ligand-dependent transcription factors, regulates the expression of important target genes. NRs control most physiological functions and are implicated in several pathological processes.

In 1995 he solved the first crystal structures of the ligand binding domains (LBDs) of two NRs of retinoids (RXR and RAR) in their apo and liganded form respectively[13][14]. These structures allowed to define a canonical unique fold for the whole family and revealed the molecular mechanism of ligand dependent activation, setting up the bases for the design of agonist and antagonist drugs[15]. The crystal structure of RXR LBD was the first determination of a protein structure using Xenon as heavy atom derivative.

His team contributed several other molecular structures of NRs LBDs, notably those of human VDR (vitamin D) and insect’s receptor Ecdysone (EcR)[16][17].

In 2004 a comparative analysis of the primary sequences lead to the partition of the superfamily into two classes according to mutually exclusive invariant aminoacids. A functional correlation with clear evolutionary implications could be made with their dimerization properties. Class I receptors encompasses homodimers or monomers while class II assembles the receptors that form heterodimers with RXR[18].

In order to decipher the structural bases of the communication between nuclear receptors, DNA and components of the basal transcription machinery he used the multi-scale approach of integrative structural biology. The solution structures of several nuclear receptors heterodimers bound to their DNA response elements was the first milestone (16). It was followed by the cryo-EM structure determination of two additional complexes (17,18).

Honors and Awards

- Bronze Medal, CNRS, 1972, silver Medal, 1982

- French Academy of Sciences, 1987

- European Molecular Biology Organization (EMBO) member, 1987

- Academia Europaea, member, 1998

- American Academy of Arts and Sciences, member, 1998

- Chevalier de l'ordre de la Légion d'honneur, 2002

- Officier dans l’Ordre National du Mérite, 2014

References

  1. ^ "Équipe Biologie structurale intégrative". Institut de génétique et de biologie moléculaire et cellulaire. Retrieved 12 April 2019.
  2. ^ Académie des sciences : Dino Moras, CV sur le site de l'Académie des sciences : www.academie-sciences.fr. Accessed 14 Feb 2013
  3. ^ Académie des sciences. "Présentation de Dino Moras". www.academie-sciences.fr (in French). Retrieved 18 February 2014.
  4. ^ Moras, D. (1968). "Crystal structure of di-(phosporyl trichloride) hexachloroditin (IV) di- u dichlorophosphate". Chem. Comm. 26.
  5. ^ Metz, B. (1970). "Crystal structure of a rubidium "cryptate"". Chem. Comm. 217.
  6. ^ Behr, J.P. (1982). "The H30+cation: molecular structure of an oxonium-macrocyclic polyether complex". J. Amer. Chem. Soc. 104: 4540–4543. doi:10.1021/ja00381a007.
  7. ^ Moras D. (1980). "3D structure of yeast tRNAAsp". Nature. 288: 669–674. doi:10.1038/288669a0.
  8. ^ Eriani, G. (1990). "Partition of tRNA-synthetases into two classes based on mutually exclusive sets of sequence motifs". Nature. 347 (6289): 203–206. Bibcode:1990Natur.347..203E. doi:10.1038/347203a0.
  9. ^ Ruff, M. (1991). "Class II aminoacyl tRNA-synthetases : crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNAAsp". Science. 252: 1682–1689. doi:10.1126/science.2047877.
  10. ^ Cavarelli, J. (1994). "The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction". EMBO J. 113 (2): 327–37.
  11. ^ Sankaranarayanan, R. (1999). "The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site". Cell. 97 (3): 371–381. doi:10.1016/S0092-8674(00)80746-1.
  12. ^ Dock-Bregeon, A-C. (2000). "Transfer RNA-Mediated editing in threonyl-tRNA synthetase : The class II solution to the double discrimination problem". Cell. 103: 1–20.
  13. ^ Bourguet, W. (1995). "Crystal structure of the Ligand Binding Domain of the Human Nuclear Receptor RXRα". Nature. 375 (6530): 377–382. Bibcode:1995Natur.375..377B. doi:10.1038/375377a0.
  14. ^ Renaud, J.-P. (1995). "Crystal Structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid". Nature. 378 (6558): 681–689. Bibcode:1995Natur.378..681R. doi:10.1038/378681a0.
  15. ^ Brelivet, Y. (2004). "Signature of the oligomeric behavior of nuclear receptors at the sequence and structural level". EMBO Reports. 5 (4): 423–429. doi:10.1038/sj.embor.7400119.
  16. ^ Rochel, N. (2000). "The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand". Mol Cell. 5: 173–179. doi:10.1016/S1097-2765(00)80413-X.
  17. ^ Billas, IM. (2003). "Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor". Nature. 426 (6962): 91–96. Bibcode:2003Natur.426...91B. doi:10.1038/nature02112.
  18. ^ Rochel, N., 2011. "Common architecture Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacing". Nat Struct Mol Biol. 18: 564–70. doi:10.1038/nsmb.2054. {{cite journal}}: |first= has numeric name (help)
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