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Article: Mutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase
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TitleMutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase
 
AuthorsWang, YX2
Zhang, HJ1
Xu, J2
Zheng, BJ1
Wen, YM2
 
Issue Date2008
 
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
 
CitationBiochemical 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.
 
ISSN0006-291X
2013 Impact Factor: 2.281
 
DOIhttp://dx.doi.org/10.1016/j.bbrc.2008.10.106
 
ISI Accession Number IDWOS: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.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorWang, YX
 
dc.contributor.authorZhang, HJ
 
dc.contributor.authorXu, J
 
dc.contributor.authorZheng, BJ
 
dc.contributor.authorWen, YM
 
dc.date.accessioned2012-08-08T08:51:01Z
 
dc.date.available2012-08-08T08:51:01Z
 
dc.date.issued2008
 
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.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationBiochemical 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
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.bbrc.2008.10.106
 
dc.identifier.epage920
 
dc.identifier.hkuros156479
 
dc.identifier.hkuros168239
 
dc.identifier.isiWOS: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.

 
dc.identifier.issn0006-291X
2013 Impact Factor: 2.281
 
dc.identifier.issue3
 
dc.identifier.pmid18976635
 
dc.identifier.scopuseid_2-s2.0-56049097627
 
dc.identifier.spage915
 
dc.identifier.urihttp://hdl.handle.net/10722/157533
 
dc.identifier.volume377
 
dc.languageeng
 
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
 
dc.publisher.placeUnited States
 
dc.relation.ispartofBiochemical and Biophysical Research Communications
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAmino Acid Motifs - Genetics
 
dc.subject.meshAmino Acid Substitution
 
dc.subject.meshCell Line
 
dc.subject.meshDna - Metabolism
 
dc.subject.meshHiv Reverse Transcriptase - Genetics - Metabolism
 
dc.subject.meshHiv-1 - Enzymology - Genetics - Physiology
 
dc.subject.meshHumans
 
dc.subject.meshMutation
 
dc.subject.meshProtein Structure, Secondary
 
dc.subject.meshVirus Replication - Genetics
 
dc.titleMutational analysis of the "turn" of helix clamp motif of HIV-1 reverse transcriptase
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Fudan University Shanghai Medical College