Proteinases of betaretroviruses bind single-stranded nucleic acids through a novel interaction module, the G-patch.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Svec M,Bauerová H,Pichová I,Konvalinka J,Strísovský K

doi

10.1016/j.febslet.2004.09.010

keywords:

subject

Has Abstract

pub_date

2004-10-08 00:00:00

pages

271-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S001457930401124X

journal_volume

576

pub_type

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