The Gag-like Protein of the Yeast Ty1 Retrotransposon Contains a Nucleic Acid Chaperone Domain Analogous to Retroviral Nucleocapsid Proteins

The reverse transcription process for retroviruses and retrotransposons takes place in a nucleocore structure in the virus or virus-like particle. In retroviruses the major protein of the nucleocore is the nucleocapsid protein (NC protein), which derives from the C-terminal region of GAG. Retroviral...

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Published inThe Journal of biological chemistry Vol. 275; no. 25; pp. 19210 - 19217
Main Authors Cristofari, Gaël, Ficheux, Damien, Darlix, Jean-Luc
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 23.06.2000
American Society for Biochemistry and Molecular Biology
Subjects
AIDS/HIV
Biochemistry, Molecular Biology
Dimerization
Gag protein
Gene Products, gag - metabolism
Life Sciences
Molecular Chaperones - metabolism
Molecular Weight
Nucleocapsid Proteins - metabolism
Retroelements
Retroviridae - metabolism
Retrovirus
Saccharomyces cerevisiae
Spumavirus
transposon Ty1
transposon Ty3
tRNA iMet
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Summary:The reverse transcription process for retroviruses and retrotransposons takes place in a nucleocore structure in the virus or virus-like particle. In retroviruses the major protein of the nucleocore is the nucleocapsid protein (NC protein), which derives from the C-terminal region of GAG. Retroviral NC proteins are formed of either one or two CCHC zinc finger(s) flanked by basic residues and have nucleic acid chaperone and match-maker properties essential for virus replication. Interestingly, the GAG protein of a number of retroelements including Spumaviruses does not possess the hallmarks of retroviral GAGs and in particular lacks a canonical NC protein. In an attempt to search for a nucleic acid chaperone activity in this class of retroelements we used the yeast Ty1 retrotransposon as a model system. Results shows that the C-terminal region of Ty1 GAG contains a nucleic acid chaperone domain capable of promoting the annealing of primer tRNAiMet to the multipartite primer binding site, Ty1 RNA dimerization and initiation of reverse transcription. Moreover Ty1 RNA dimerization, in a manner similar to Ty3 but unlike retroviral RNAs, appears to be mediated by tRNAiMet. These findings suggest that nucleic acid chaperone proteins probably are general co-factors for reverse transcriptases.
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M001371200