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Article: Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase

TitleSirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
Authors
KeywordsNicotinamide adenine dinucleotide
Phosphorus 32
Sirtuin
Enzyme activity
Mass spectrometry
Issue Date2011
PublisherAmerican Association for the Advancement of Science. The Journal's web site is located at http://sciencemag.org
Citation
Science, 2011, v. 334 n. 6057, p. 806-809 How to Cite?
Abstract
Silent information regulator 2 (Sir2) proteins (sirtuins) are nicotinamide adenine dinucleotide-dependent deacetylases that regulate important biological processes. Mammals have seven sirtuins, Sirt1 to Sirt7. Four of them (Sirt4 to Sirt7) have no detectable or very weak deacetylase activity. We found that Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro. The preference for succinyl and malonyl groups was explained by the presence of an arginine residue (Arg 105) and tyrosine residue (Tyr 102) in the acyl pocket of Sirt5. Several mammalian proteins were identified with mass spectrometry to have succinyl or malonyl lysine modifications. Deletion of Sirt5 in mice appeared to increase the level of succinylation on carbamoyl phosphate synthase 1, which is a known target of Sirt5. Thus, protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo.
Persistent Identifierhttp://hdl.handle.net/10722/145585
ISSN
2013 Impact Factor: 31.477
2013 SCImago Journal Rankings: 12.465
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Dreyfus Foundation
NIHR01GM086703
RR01646
Hong KongGRF766510
NIH PPGDK58920
European UnionERC-2008-AdG-23118
Ecole Polytechnique Federale de Lausanne
Funding Information:

This work is supported in part by Dreyfus Foundation (H.L.); grants NIH R01GM086703 (H.L.), Hong Kong GRF766510 (Q.H.), NIH RR01646 (R.A.C. and Q.H.), and NIH PPG DK58920 (J.A.); the European Union Ideas program (sirtuins; ERC-2008-AdG-23118 to J.A.); and the Ecole Polytechnique Federale de Lausanne (J.A.). Atomic coordinates and structure factors were deposited in the Protein Data Bank (accession codes 3RIG and 3RIY).

References

 

Author Affiliations
  1. Cornell University
  2. The University of Hong Kong
  3. Ecole Polytechnique Federale de Lausanne
DC FieldValueLanguage
dc.contributor.authorDu, Jen_HK
dc.contributor.authorZhou, Yen_HK
dc.contributor.authorSu, Xen_HK
dc.contributor.authorYu, JJen_HK
dc.contributor.authorKhan, Sen_HK
dc.contributor.authorJiang, Hen_HK
dc.contributor.authorKim, Jen_HK
dc.contributor.authorWoo, Jen_HK
dc.contributor.authorKim, JHen_HK
dc.contributor.authorChoi, BHen_HK
dc.contributor.authorHe, Ben_HK
dc.contributor.authorChen, Wen_HK
dc.contributor.authorZhang, Sen_HK
dc.contributor.authorCerione, RAen_HK
dc.contributor.authorAuwerx, Jen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorLin, Hen_HK
dc.date.accessioned2012-02-28T01:55:54Z-
dc.date.available2012-02-28T01:55:54Z-
dc.date.issued2011en_HK
dc.identifier.citationScience, 2011, v. 334 n. 6057, p. 806-809en_HK
dc.identifier.issn0036-8075en_HK
dc.identifier.urihttp://hdl.handle.net/10722/145585-
dc.description.abstractSilent information regulator 2 (Sir2) proteins (sirtuins) are nicotinamide adenine dinucleotide-dependent deacetylases that regulate important biological processes. Mammals have seven sirtuins, Sirt1 to Sirt7. Four of them (Sirt4 to Sirt7) have no detectable or very weak deacetylase activity. We found that Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro. The preference for succinyl and malonyl groups was explained by the presence of an arginine residue (Arg 105) and tyrosine residue (Tyr 102) in the acyl pocket of Sirt5. Several mammalian proteins were identified with mass spectrometry to have succinyl or malonyl lysine modifications. Deletion of Sirt5 in mice appeared to increase the level of succinylation on carbamoyl phosphate synthase 1, which is a known target of Sirt5. Thus, protein lysine succinylation may represent a posttranslational modification that can be reversed by Sirt5 in vivo.en_HK
dc.languageengen_US
dc.publisherAmerican Association for the Advancement of Science. The Journal's web site is located at http://sciencemag.orgen_HK
dc.relation.ispartofScienceen_HK
dc.rightsScience. Copyright © American Association for the Advancement of Science.-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectNicotinamide adenine dinucleotide-
dc.subjectPhosphorus 32-
dc.subjectSirtuin-
dc.subjectEnzyme activity-
dc.subjectMass spectrometry-
dc.titleSirt5 is a NAD-dependent protein lysine demalonylase and desuccinylaseen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturepostprint-
dc.identifier.doi10.1126/science.1207861en_HK
dc.identifier.pmid22076378en_HK
dc.identifier.pmcidPMC3217313-
dc.identifier.scopuseid_2-s2.0-81055122671en_HK
dc.identifier.hkuros198782en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-81055122671&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume334en_HK
dc.identifier.issue6057en_HK
dc.identifier.spage806en_HK
dc.identifier.epage809en_HK
dc.identifier.eissn1095-9203-
dc.identifier.isiWOS:000296849600047-
dc.publisher.placeUnited Statesen_HK
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dc.identifier.scopusauthoridDu, J=7402575327en_HK
dc.identifier.scopusauthoridZhou, Y=54419337500en_HK
dc.identifier.scopusauthoridSu, X=36673908200en_HK
dc.identifier.scopusauthoridYu, JJ=54419288600en_HK
dc.identifier.scopusauthoridKhan, S=54418868400en_HK
dc.identifier.scopusauthoridJiang, H=27171339900en_HK
dc.identifier.scopusauthoridKim, J=38461284800en_HK
dc.identifier.scopusauthoridWoo, J=54419215500en_HK
dc.identifier.scopusauthoridKim, JH=54418881300en_HK
dc.identifier.scopusauthoridChoi, BH=36678646600en_HK
dc.identifier.scopusauthoridHe, B=24824492500en_HK
dc.identifier.scopusauthoridChen, W=54418491100en_HK
dc.identifier.scopusauthoridZhang, S=36183596600en_HK
dc.identifier.scopusauthoridCerione, RA=7102225792en_HK
dc.identifier.scopusauthoridAuwerx, J=7101942868en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridLin, H=8686527600en_HK
dc.identifier.citeulike10016982-

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