Format

Send to

Choose Destination
See comment in PubMed Commons below
J Virol. 1988 Apr;62(4):1433-6.

Processing protease and reverse transcriptase from human immunodeficiency virus type I polyprotein in Escherichia coli.

Author information

1
Central Research Units, F. Hoffmann-La Roche Ltd., Basel, Switzerland.

Abstract

Expression of the human immunodeficiency virus type I pol open reading frame in Escherichia coli led to several protease-mediated processing steps of the pol precursor polyprotein. Accumulation of two polypeptides with molecular sizes of 64 and 52 kilodaltons, with which reverse transcriptase activity is associated, was observed. The protease moiety of the precursor polyprotein accumulated as a 10-kilodalton species as a result of two specific cleavages. Furthermore, a single-amino-acid substitution in the putative active site of protease totally abolished processing of the precursor polyprotein.

PMID:
2450209
PMCID:
PMC253157
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center