Proteinases of betaretroviruses bind single-stranded nucleic acids through a novel interaction module, the G-patch
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15474050
DOI
10.1016/j.febslet.2004.09.010
PII: S001457930401124X
Knihovny.cz E-resources
- MeSH
- Amino Acid Motifs MeSH
- Betaretrovirus enzymology MeSH
- Point Mutation MeSH
- Glycine chemistry MeSH
- DNA, Single-Stranded metabolism MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Consensus Sequence MeSH
- Conserved Sequence MeSH
- Mason-Pfizer monkey virus metabolism MeSH
- Molecular Sequence Data MeSH
- Peptide Hydrolases chemistry genetics metabolism MeSH
- Recombinant Proteins isolation & purification metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Protein Structure, Tertiary * MeSH
- Tyrosine chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Glycine MeSH
- DNA, Single-Stranded MeSH
- Peptide Hydrolases MeSH
- Recombinant Proteins MeSH
- Tyrosine MeSH
Retroviral proteinases (PRs) are essential for retrovirus infectivity but the mechanism of their activity regulation is poorly understood. We investigated possible involvement in this process of the C-terminal domain (CTD) of betaretroviral PRs. We found that the presence of CTD attenuates proteolytic activity of Mason-Pfizer monkey virus PR, while it does not significantly affect the activity of mouse intracisternal A-particle retrovirus PR. However, both PRs bind single-stranded nucleic acids through their CTDs that contain a novel binding motif, the G-patch, whose function is dependent on a single conserved tyrosine residue. Oligonucleotide binding to both PRs does not inhibit their proteolytic activity.
References provided by Crossref.org
The G-patch domain of Mason-Pfizer monkey virus is a part of reverse transcriptase
