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.
Svec
Martin
M
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.
Bauerová
Helena
H
Pichová
Iva
I
Konvalinka
Jan
J
Strísovský
Kvido
K
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