Format

Send to

Choose Destination
See comment in PubMed Commons below
Semin Cell Dev Biol. 2000 Feb;11(1):35-44.

Intramolecular chaperones: polypeptide extensions that modulate protein folding.

Author information

1
Department of Biochemistry, UMDNJ-RWJMS, 675 Hoes Lane, Piscataway, NJ 08854, USA.

Abstract

Several prokaryotic and eukaryotic proteins are synthesized as precursors in the form of pre-pro-proteins. While the pre-regions function as signal peptides that are involved in transport, the propeptides can often catalyze correct folding of their associated proteins. Such propeptides have been termed intramolecular chaperones. In cases where propeptides may not directly catalyze the folding reaction, it appears that they can facilitate processes such as structural organization and oligomerization, localization, sorting and modulation of enzymatic activity and stability of proteins. Based on the available literature it appears that propeptides may actually function as 'post-translational modulators' of protein structure and function. Propeptides can be classified into two broad categories: Class I propeptides that function as intramolecular chaperones and directly catalyze the folding reaction; and Class II propeptides that are not directly involved in folding.

PMID:
10736262
DOI:
10.1006/scdb.1999.0349
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center