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Article: Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
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TitlePlasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
 
AuthorsZhu, AY1
Zhou, Y1
Khan, S1
Deitsch, KW2
Hao, Q1 3
Lin, H1
 
Issue Date2012
 
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/acbcct/index.html
 
CitationAcs Chemical Biology, 2012, v. 7 n. 1, p. 155-159 [How to Cite?]
DOI: http://dx.doi.org/10.1021/cb200230x
 
AbstractPlasmodium falciparum Sir2A (PfSir2A), a member of the sirtuin family of nicotinamide adenine dinucleotide-dependent deacetylases, has been shown to regulate the expression of surface antigens to evade the detection by host immune surveillance. It is thought that PfSir2A achieves this by deacetylating histones. However, the deacetylase activity of PfSir2A is weak. Here we present enzymology and structural evidence supporting that PfSir2A catalyzes the hydrolysis of medium and long chain fatty acyl groups from lysine residues more efficiently. Furthermore, P. falciparum proteins are found to contain such fatty acyl lysine modifications that can be removed by purified PfSir2A in vitro. Together, the data sugget that the physiological function of PfSir2A in antigen variation may be achieved by removing medium and long chain fatty acyl groups from protein lysine residues. The robust activity of PfSir2A would also facilitate the development of PfSir2A inhibitors, which may have therapeutic value in malaria treatment. © 2011 American Chemical Society.
 
ISSN1554-8929
2013 Impact Factor: 5.356
 
DOIhttp://dx.doi.org/10.1021/cb200230x
 
PubMed Central IDPMC3262940
 
ISI Accession Number IDWOS:000299241300016
Funding AgencyGrant Number
NIHR01GM086703
RR01646
T32 GM08500
Hong KongGRF766510
Funding Information:

This work is supported in part by NIH R01GM086703 (H.L.), NIH RR01646 (Q.H.), and Hong Kong GRF766510 (Q.H.). A.Y.Z. is a CBI training grant trainee (NIH T32 GM08500).

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorZhu, AY
 
dc.contributor.authorZhou, Y
 
dc.contributor.authorKhan, S
 
dc.contributor.authorDeitsch, KW
 
dc.contributor.authorHao, Q
 
dc.contributor.authorLin, H
 
dc.date.accessioned2012-02-28T01:55:53Z
 
dc.date.available2012-02-28T01:55:53Z
 
dc.date.issued2012
 
dc.description.abstractPlasmodium falciparum Sir2A (PfSir2A), a member of the sirtuin family of nicotinamide adenine dinucleotide-dependent deacetylases, has been shown to regulate the expression of surface antigens to evade the detection by host immune surveillance. It is thought that PfSir2A achieves this by deacetylating histones. However, the deacetylase activity of PfSir2A is weak. Here we present enzymology and structural evidence supporting that PfSir2A catalyzes the hydrolysis of medium and long chain fatty acyl groups from lysine residues more efficiently. Furthermore, P. falciparum proteins are found to contain such fatty acyl lysine modifications that can be removed by purified PfSir2A in vitro. Together, the data sugget that the physiological function of PfSir2A in antigen variation may be achieved by removing medium and long chain fatty acyl groups from protein lysine residues. The robust activity of PfSir2A would also facilitate the development of PfSir2A inhibitors, which may have therapeutic value in malaria treatment. © 2011 American Chemical Society.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationAcs Chemical Biology, 2012, v. 7 n. 1, p. 155-159 [How to Cite?]
DOI: http://dx.doi.org/10.1021/cb200230x
 
dc.identifier.doihttp://dx.doi.org/10.1021/cb200230x
 
dc.identifier.epage159
 
dc.identifier.hkuros198781
 
dc.identifier.isiWOS:000299241300016
Funding AgencyGrant Number
NIHR01GM086703
RR01646
T32 GM08500
Hong KongGRF766510
Funding Information:

This work is supported in part by NIH R01GM086703 (H.L.), NIH RR01646 (Q.H.), and Hong Kong GRF766510 (Q.H.). A.Y.Z. is a CBI training grant trainee (NIH T32 GM08500).

 
dc.identifier.issn1554-8929
2013 Impact Factor: 5.356
 
dc.identifier.issue1
 
dc.identifier.pmcidPMC3262940
 
dc.identifier.pmid21992006
 
dc.identifier.scopuseid_2-s2.0-84862907582
 
dc.identifier.spage155
 
dc.identifier.urihttp://hdl.handle.net/10722/145584
 
dc.identifier.volume7
 
dc.languageeng
 
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/acbcct/index.html
 
dc.publisher.placeUnited States
 
dc.relation.ispartofACS Chemical Biology
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshHistones - metabolism
 
dc.subject.meshLysine - metabolism
 
dc.subject.meshPlasmodium falciparum - enzymology - genetics - immunology
 
dc.subject.meshProtozoan Proteins - chemistry - genetics - metabolism
 
dc.subject.meshSirtuins - chemistry - genetics - metabolism
 
dc.titlePlasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
 
dc.typeArticle
 
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Author Affiliations
  1. Cornell University
  2. Weill Cornell Medical College
  3. The University of Hong Kong