4axp: Difference between revisions
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==NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.== | ==NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.== | ||
<StructureSection load='4axp' size='340' side='right' caption='[[4axp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='4axp' size='340' side='right'caption='[[4axp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4axp]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4axp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AXP FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4axp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4axp OCA], [https://pdbe.org/4axp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4axp RCSB], [https://www.ebi.ac.uk/pdbsum/4axp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4axp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/HSP12_YEAST HSP12_YEAST]] May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Heat Shock | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Bloxam, L]] | [[Category: Bloxam, L]] | ||
[[Category: Herbert, A P]] | [[Category: Herbert, A P]] | ||
Latest revision as of 08:49, 25 August 2022
NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.
Structural highlights
Function[HSP12_YEAST] May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism. Publication Abstract from PubMedDietary restriction (DR) extends lifespan in yeast, worms, flies and mammals, suggesting that it may act via conserved processes. However, the downstream mechanisms by which DR increases lifespan remain unclear. We used a gel based proteomic strategy to identify proteins whose expression was induced by DR in yeast and thus may correlate with longevity. One protein up-regulated by DR was Hsp12, a small heat shock protein induced by various manipulations known to retard ageing. Lifespan extension by growth on 0.5% glucose (DR) was abolished in an hsp12Delta strain, indicating that Hsp12 is essential for the longevity effect of DR. In contrast, deletion of HSP12 had no effect on growth under DR conditions or a variety of environmental stresses, indicating that the effect of Hsp12 on lifespan is not due to increased general stress resistance. Unlike other small heat shock proteins, recombinant Hsp12 displayed negligible in vitro molecular chaperone activity, suggesting that its cellular function does not involve preventing protein aggregation. NMR analysis indicated that Hsp12 is monomeric and intrinsically unfolded in solution, but switches to a 4-helical conformation upon binding to membrane-mimetic SDS micelles. The structure of micelle-bound Hsp12 reported here is consistent with its recently proposed function as a membrane-stabilising 'lipid chaperone'. Taken together, our data suggest that DR-induced Hsp12 expression contributes to lifespan extension, possibly via membrane alterations. NMR structure of hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast.,Herbert AP, Riesen M, Bloxam L, Kosmidou E, Wareing BM, Johnson JR, Phelan MM, Pennington SR, Lian LY, Morgan A PLoS One. 2012;7(7):e41975. Epub 2012 Jul 27. PMID:22848679[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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