File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine

TitlePlasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
Authors
Issue Date2012
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/acbcct/index.html
Citation
Acs Chemical Biology, 2012, v. 7 n. 1, p. 155-159 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/145584
ISSN
2014 Impact Factor: 5.331
PubMed Central ID
ISI Accession Number ID
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).

References

 

DC FieldValueLanguage
dc.contributor.authorZhu, AYen_HK
dc.contributor.authorZhou, Yen_HK
dc.contributor.authorKhan, Sen_HK
dc.contributor.authorDeitsch, KWen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorLin, Hen_HK
dc.date.accessioned2012-02-28T01:55:53Z-
dc.date.available2012-02-28T01:55:53Z-
dc.date.issued2012en_HK
dc.identifier.citationAcs Chemical Biology, 2012, v. 7 n. 1, p. 155-159en_HK
dc.identifier.issn1554-8929en_HK
dc.identifier.urihttp://hdl.handle.net/10722/145584-
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.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/acbcct/index.htmlen_HK
dc.relation.ispartofACS Chemical Biologyen_HK
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 lysineen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1021/cb200230xen_HK
dc.identifier.pmid21992006en_HK
dc.identifier.pmcidPMC3262940-
dc.identifier.scopuseid_2-s2.0-84862907582en_HK
dc.identifier.hkuros198781en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84862907582&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume7en_HK
dc.identifier.issue1en_HK
dc.identifier.spage155en_HK
dc.identifier.epage159en_HK
dc.identifier.isiWOS:000299241300016-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhu, AY=55264623200en_HK
dc.identifier.scopusauthoridZhou, Y=49562143100en_HK
dc.identifier.scopusauthoridKhan, S=54418868400en_HK
dc.identifier.scopusauthoridDeitsch, KW=6602154433en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridLin, H=8686527600en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats