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Cited by 32HIV Research and TreatmentHIV/AIDS drug development and treatmentT-cell and Retrovirus Studies

The DOI matches its Crossref record, with a small difference in title or year; 53 of the 53 references it cites were found in a registry or an index.

A HIV-1 Minimal Gag Protein Is Superior to Nucleocapsid at in Vitro tRNA3Lys Annealing and Exhibits Multimerization-induced Inhibition of Reverse Transcription

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Roldan, Ariel, Warren, Otis U., Russell, Rodney S., Liang, Chen, Wainberg, Mark A.·2005·Journal of Biological Chemistry
DOI 10.1074/jbc.m501310200
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Abstract

HIV-1 uses tRNA3Lys to prime reverse transcription of its viral RNA. In this process, the 3'-end of tRNA3Lys must be annealed to the primer binding site of HIV-1 genomic RNA, and the two molecules together form a complex structure. During annealing, the nucleocapsid (NC) protein enhances the unwinding of tertiary structures within both RNA molecules. Moreover, the packaging of tRNA3Lys occurs prior to viral budding at a time when NC is still part of the Pr55Gag polyprotein. In contrast, Pr55Gag is able to produce virus-like particles on its own. We have recently shown that an N-terminal extended form of NC (mGag), containing all of the minimal elements required for virus-like particle formation, possesses greater affinity for HIV-1 genomic RNA than does NC alone. We have now studied the tRNA3Lys-annealing properties of mGag in comparison to those of NC and report that the former is more efficient in this regard than the latter. We have also tested each of a mutant version of mGag, an extended form of mGag, and an almost full-length form of Gag, and showed that all of these possessed greater tRNA-annealing capacity than did the viral NC protein. Yet, surprisingly, multimerization of Gag-related proteins did not abrogate this annealing process but rather resulted in dramatically reduced levels of reverse transcriptase processivity. These results suggest that the initial stages of reverse transcription may be regulated by the multimerization of Pr55Gag polyprotein at times prior to the cleavage of NC.

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Crossref · 10.1074/jbc.m501310200

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  • Annealing of tRNA Lys,3 to the HIV-1 PBS can be facilitated by either the Gag polyprotein or the mature NC protein in vitro.

    “Annealing of tRNA Lys,3 to the HIV-1 PBS can be facilitated by either the Gag polyprotein or the mature NC protein in vitro (38,39).”

    From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [39]

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Metadata

Authors
Roldan, A., Warren, O. U., Russell, R. S., Liang, C., & Wainberg, M. A.
Affiliations
Jewish General Hospital (CA)
Corresponding author
Wainberg, Mark A.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2005-04
Volume
280
Issue
17
Pages
17488-17496
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m501310200
OpenAlex
W2099754066
Cited by
29
References
53
Citations by year
2026: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 3 · 2017: 2 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 3
FWCI
0.34
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords
HIV-1, nucleocapsid protein, Pr55gag, reverse transcription, primer binding site, RNA annealing, multimerization, virus-like particles, RNA tertiary structure
MeSH terms
DNA, Dose-Response Relationship, Drug, Hot Temperature, Models, Biological, Models, Genetic, Mutation, Nucleic Acid Conformation, Protein Binding, Protein Precursors, Proteins, RNA, RNA, Transfer, RNA, Transfer, Amino Acyl, Transcription, Genetic, HIV-1, Gene Products, gag, Polymerase Chain Reaction, Protein Structure, Tertiary, Protein Folding, DNA Primers, Nucleocapsid, Dimerization, In Vitro Techniques

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