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Article: Mutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase

TitleMutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase
Authors
Wang, YXZhang, HJXu, JZheng, BJWen, YM
KeywordsHIV-1
Polymerase activity
Processivity
Replication
Reverse transcriptase
Turn of helix clamp motif
Issue Date2008
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 2008, v. 377 n. 3, p. 915-920 How to Cite?
DOI: http://dx.doi.org/10.1016/j.bbrc.2008.10.106
AbstractHelix clamp motifs of polymerases possessing the helix-turn-helix secondary structure are crucial for their polymerase activity by binding to the nucleic acid template/primer via the alpha helices. To study the functions of turn in helix clamp motif of human immunodeficiency virus (HIV)-1 RT, clones with turn mutants at rt271-274 of HIV-1 RT were generated and studied by one cycle infection assay. Mutants rtY271A and rtI274A almost lost their replication competency, while mutants rtA272P, rtA272S, and rtG273A retained comparable replication competency relative to wild type pseudotyped HIV-1. To study the mechanisms involved, RT proteins from rt271 to rt274 mutants were expressed and assayed for their RNA dependent DNA polymerase activity, DNA binding activity and processivity. Discordance between RT activity and viral replication efficiency of some turn mutants was observed, indicating that aside from RT, other steps in HIV replication could be affected by substitutions at the turn of helix clamp motif. © 2008 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/157533
ISSN
0006-291X
2021 Impact Factor: 3.322
2020 SCImago Journal Rankings: 0.998
ISI Accession Number ID
WOS:000261458900034
Funding AgencyGrant Number
Shanghai Educational Development FoundationKBF101038
NSFC30800048
Sino-Germen Grant GZ230202/3
Shanghai Municipal Government Basic Research05JC14008
AIDS Trust Fund of Hong Kong SAR Government
Funding Information:

Jurkat Clone E6-1, pHEF-VSVG, and pNL4-3-deltaE-EGFP were kindly provided by the AIDS Research and Reference Reagent Program. This study was supported in part by Grants from 973 (G1999054105), Shanghai Educational Development Foundation (KBF101038), NSFC (30800048), Sino-Germen Grant GZ230 (202/3), Shanghai Municipal Government Basic Research (05JC14008), and the AIDS Trust Fund of Hong Kong SAR Government.

References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorWang, YXen_US
dc.contributor.authorZhang, HJen_US
dc.contributor.authorXu, Jen_US
dc.contributor.authorZheng, BJen_US
dc.contributor.authorWen, YMen_US
dc.date.accessioned2012-08-08T08:51:01Z-
dc.date.available2012-08-08T08:51:01Z-
dc.date.issued2008en_US
dc.identifier.citationBiochemical And Biophysical Research Communications, 2008, v. 377 n. 3, p. 915-920en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/157533-
dc.description.abstractHelix clamp motifs of polymerases possessing the helix-turn-helix secondary structure are crucial for their polymerase activity by binding to the nucleic acid template/primer via the alpha helices. To study the functions of turn in helix clamp motif of human immunodeficiency virus (HIV)-1 RT, clones with turn mutants at rt271-274 of HIV-1 RT were generated and studied by one cycle infection assay. Mutants rtY271A and rtI274A almost lost their replication competency, while mutants rtA272P, rtA272S, and rtG273A retained comparable replication competency relative to wild type pseudotyped HIV-1. To study the mechanisms involved, RT proteins from rt271 to rt274 mutants were expressed and assayed for their RNA dependent DNA polymerase activity, DNA binding activity and processivity. Discordance between RT activity and viral replication efficiency of some turn mutants was observed, indicating that aside from RT, other steps in HIV replication could be affected by substitutions at the turn of helix clamp motif. © 2008 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_US
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_US
dc.subjectHIV-1-
dc.subjectPolymerase activity-
dc.subjectProcessivity-
dc.subjectReplication-
dc.subjectReverse transcriptase-
dc.subjectTurn of helix clamp motif-
dc.subject.meshAmino Acid Motifs - Geneticsen_US
dc.subject.meshAmino Acid Substitutionen_US
dc.subject.meshCell Lineen_US
dc.subject.meshDna - Metabolismen_US
dc.subject.meshHiv Reverse Transcriptase - Genetics - Metabolismen_US
dc.subject.meshHiv-1 - Enzymology - Genetics - Physiologyen_US
dc.subject.meshHumansen_US
dc.subject.meshMutationen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshVirus Replication - Geneticsen_US
dc.titleMutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptaseen_US
dc.typeArticleen_US
dc.identifier.emailZheng, BJ:bzheng@hkucc.hku.hken_US
dc.identifier.authorityZheng, BJ=rp00353en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.bbrc.2008.10.106en_US
dc.identifier.pmid18976635-
dc.identifier.scopuseid_2-s2.0-56049097627en_US
dc.identifier.hkuros156479-
dc.identifier.hkuros168239-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-56049097627&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume377en_US
dc.identifier.issue3en_US
dc.identifier.spage915en_US
dc.identifier.epage920en_US
dc.identifier.isiWOS:000261458900034-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridWang, YX=9942220100en_US
dc.identifier.scopusauthoridZhang, HJ=14124271200en_US
dc.identifier.scopusauthoridXu, J=7407003499en_US
dc.identifier.scopusauthoridZheng, BJ=7201780588en_US
dc.identifier.scopusauthoridWen, YM=7401776949en_US
dc.identifier.issnl0006-291X-

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