You are not logged in.
Openly accessible

Analysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation

Buxton, Penelope, Tachedjian, Gilda and Mak, Johnson 2005, Analysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation, Journal of virology, vol. 79, no. 10, pp. 6338-6348.

Attached Files
Name Description MIMEType Size Downloads
mak-analysisofthe-2005.pdf Published version application/pdf 549.57KB 28

Title Analysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation
Author(s) Buxton, Penelope
Tachedjian, Gilda
Mak, JohnsonORCID iD for Mak, Johnson orcid.org/0000-0002-5229-5707
Journal name Journal of virology
Volume number 79
Issue number 10
Start page 6338
End page 6348
Total pages 11
Publisher American Society for Microbiology
Place of publication Washington, D. C.
Publication date 2005-05
ISSN 0022-538X
1098-5514
Keyword(s) retrovirus
genomic RNA
HIV-1
proteins
RNA dimer conformation
reverse transcriptase
Summary All retroviruses contain two copies of genomic RNA that are linked noncovalently. The dimeric RNA of human immunodeficiency virus type 1 (HIV-1) undergoes rearrangement during virion maturation, whereby the dimeric RNA genome assumes a more stable conformation. Previously, we have shown that the packaging of the HIV-1 polymerase (Pol) proteins reverse transcriptase (RT) and integrase (IN) is essential for the generation of the mature RNA dimer conformation. Analysis of HIV-1 mutants that are defective in processing of Pol showed that these mutant virions contained altered dimeric RNA conformation, indicating that the mature RNA dimer conformation in HIV-1 requires the correct proteolytic processing of Pol. The HIV-1 Pol proteins are multimeric in their mature enzymatically active forms; RT forms a heterodimer, and IN appears to form a homotetramer. Using RT and IN multimerization defective mutants, we have found that dimeric RNA from these mutant virions has the same stability and conformation as wild-type RNA dimers, showing that the mature enzymatically active RT and IN proteins are dispensable for the generation of mature RNA dimer conformation. This also indicated that formation of the mature RNA dimer structure occurs prior to RT or IN maturation. We have also investigated the requirement of Pol for RNA dimerization in both Mason-Pfizer monkey virus (M-PMV) and Moloney murine leukemia virus (MoMuLV) and found that in contrast to HIV-1, Pol is dispensable for RNA dimer maturation in M-PMV and MoMuLV, demonstrating that the requirement of Pol in retroviral RNA dimer maturation is not conserved among all retroviruses.
Language eng
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2005, American Society for Microbiology
Persistent URL http://hdl.handle.net/10536/DRO/DU:30047541

Document type: Journal Article
Collections: School of Medicine
Open Access Collection
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 0 times in TR Web of Science
Scopus Citation Count Cited 17 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 183 Abstract Views, 29 File Downloads  -  Detailed Statistics
Created: Thu, 30 Aug 2012, 09:41:22 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.