Late embryogenesis abundant proteins: Difference between revisions
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'''Late [[Embryogenesis]] Abundant''' [[protein]]s ('''LEA proteins''') are proteins in animals and plants that protect other proteins from aggregation from [[desiccation]] or [[osmotic shock|osmotic stresses]] associated with low temperature.<ref name="Goyal">{{cite journal | author=Goyal, K., Walton, L. J., & Tunnacliffe, A. | title=LEA proteins prevent protein aggregation due to water stress | quotes=no | journal=Biochemical Journal | year=2005 | volume=388 | issue=Part 1 | pages= |
'''Late [[Embryogenesis]] Abundant''' [[protein]]s ('''LEA proteins''') are proteins in animals and plants that protect other proteins from aggregation from [[desiccation]] or [[osmotic shock|osmotic stresses]] associated with low temperature.<ref name="Goyal">{{cite journal | author=Goyal, K., Walton, L. J., & Tunnacliffe, A. | title=LEA proteins prevent protein aggregation due to water stress | quotes=no | journal=Biochemical Journal | year=2005 | volume=388 | issue=Part 1 | pages=151–157 |url=http://www.biochemj.org/bj/388/0151/bj3880151.htm |archiveurl=http://www.webcitation.org/5il9QhYT0 |archivedate=2010-04-03 | format = [[HTML]] | pmid=15631617 | doi=10.1042/BJ20041931 | pmc=1186703}}</ref> LEA proteins were initially discovered accumulating late in embryogenesis of [[Gossypium|cotton]] [[seed]]s.<ref>{{cite journal | author=Dure L 3rd, Greenway SC, Galau GA | title=Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis | quotes=no | journal=Biochemistry | year=1981 | volume=7 | issue=14 | pages=4162-4168 | pmid=7284317 }}</ref> Although abundant in seeds and pollens, LEA proteins have been found to protect against desiccation in a variety of organisms, including the [[Bacteria|bacterium]] ''[[Deinococcus radiodurans]]'', [[nematode]] ''[[Caenorhabditis elegans]]'', and [[rotifer]]s.<ref>{{cite journal | author=Hundertmark M, Hincha DK | title=An LEA group 3 family member is involved in survival of C. elegans during exposure to stress | journal=FEBS Letters | volume=577 | issue=1-2 | year=2004 | pages=21-26 | format = [[HTML]] | id=PMID 15527756 }}</ref><ref>{{cite journal | author=Goyal, K., Walton, L. J., & Tunnacliffe, A. | title=LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana | quotes=no | journal=BMC Genomics | year=2008 | volume=9 | pages=118 |url=http://www.biomedcentral.com/1471-2164/9/118 format = [[HTML]] | pmid=18318901 }}</ref> |
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LEA proteins function by mechanisms which are distinct from those displayed by [[heat shock]] [[Chaperone (protein)|molecular chaperones]].<ref name="Goyal" /> Although the causes of LEA protein induction have not yet been determined, conformational changes in [[transcription factor]]s or [[integral membrane protein]]s due to water loss have been suggested.<ref>{{cite journal | author=Caramelo JJ, Iusem ND | title=When cells lose water: Lessons from biophysics and molecular biology | journal=PROGRESS IN BIOPHYSICS AND MOLECULAR BIOLOGY | volume=99 | issue=1 | year=2009 | pages=1-6 | format = [[HTML]] | id=PMID 18977383}}</ref> |
LEA proteins function by mechanisms which are distinct from those displayed by [[heat shock]] [[Chaperone (protein)|molecular chaperones]].<ref name="Goyal" /> Although the causes of LEA protein induction have not yet been determined, conformational changes in [[transcription factor]]s or [[integral membrane protein]]s due to water loss have been suggested.<ref>{{cite journal | author=Caramelo JJ, Iusem ND | title=When cells lose water: Lessons from biophysics and molecular biology | journal=PROGRESS IN BIOPHYSICS AND MOLECULAR BIOLOGY | volume=99 | issue=1 | year=2009 | pages=1-6 | format = [[HTML]] | id=PMID 18977383}}</ref> |
Revision as of 02:36, 31 July 2010
Late Embryogenesis Abundant proteins (LEA proteins) are proteins in animals and plants that protect other proteins from aggregation from desiccation or osmotic stresses associated with low temperature.[1] LEA proteins were initially discovered accumulating late in embryogenesis of cotton seeds.[2] Although abundant in seeds and pollens, LEA proteins have been found to protect against desiccation in a variety of organisms, including the bacterium Deinococcus radiodurans, nematode Caenorhabditis elegans, and rotifers.[3][4]
LEA proteins function by mechanisms which are distinct from those displayed by heat shock molecular chaperones.[1] Although the causes of LEA protein induction have not yet been determined, conformational changes in transcription factors or integral membrane proteins due to water loss have been suggested.[5]
See also
References
- ^ a b Goyal, K., Walton, L. J., & Tunnacliffe, A. (2005). "LEA proteins prevent protein aggregation due to water stress". Biochemical Journal. 388 (Part 1): 151–157. doi:10.1042/BJ20041931. PMC 1186703. PMID 15631617. Archived from the original (HTML) on 2010-04-03.
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