Intramolecular chaperones: Polypeptide extensions that modulate protein folding

Ujwal Shinde, Masayori Inouye

Research output: Contribution to journalArticle

125 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)35-44
Number of pages10
JournalSeminars in Cell and Developmental Biology
Volume11
Issue number1
DOIs
StatePublished - 2000
Externally publishedYes

Fingerprint

Protein Folding
Peptides
Proteins
Protein Stability
Protein Sorting Signals

Keywords

  • Intramolecular chaperones
  • Propeptides
  • Proteases
  • Protein folding
  • Subtilisin

ASJC Scopus subject areas

  • Developmental Biology

Cite this

Intramolecular chaperones : Polypeptide extensions that modulate protein folding. / Shinde, Ujwal; Inouye, Masayori.

In: Seminars in Cell and Developmental Biology, Vol. 11, No. 1, 2000, p. 35-44.

Research output: Contribution to journalArticle

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