Proteinases of betaretroviruses bind single-stranded nucleic acids through a novel interaction module, the G-patch.
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.
Department of Protein Biochemistry, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo n. 2, Praha 6, 166 10, Czech Republic.
Martin
M
Svec
Helena
H
Bauerová
Iva
I
Pichová
Jan
J
Konvalinka
Kvido
K
Strísovský
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D030121:Betaretrovirus / Q000201:enzymology*; D016384:Consensus Sequence; D017124:Conserved Sequence; D004277:DNA, Single-Stranded / Q000378:metabolism*; D005998:Glycine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D016093:Mason-Pfizer monkey virus / Q000378:metabolism*; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017354:Point Mutation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000737:chemistry
D004277:DNA, Single-Stranded; D011994:Recombinant Proteins; D014443:Tyrosine; D010447:Peptide Hydrolases; D005998:Glycine