Tsp: A tail-specific protease that selectively degrades proteins with nonpolar C termini

Karen R. Silber, Kenneth Charles Keiler, Robert T. Sauer

Research output: Contribution to journalArticle

145 Citations (Scopus)

Abstract

An Escherichia coli protease designated Tsp (tail-specific protease) has been purified, and its gene has been cloned and sequenced. Tsp specifically degrades a variant of the N-terminal domain of A represser in which the five C-terminal residues, which are polar in wild type, have been replaced by nonpolar residues. This substrate specificity in vitro parallels the previously reported selective degradation in vivo of N-terminal-domain variants with nonpolar C-terminal residues. The gene sequence and N-terminal protein sequence of Tsp predict a protein of 660 amino acids. The deduced protein sequence of Tsp shows no significant homology to known protease sequences but does show sequence similarity to the human and bovine interphotoreceptor retinoid-binding proteins, which bind hydrophobic ligands.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number1
DOIs
StatePublished - Jan 1 1992

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Proteins
Substrate Specificity
Genes
Peptide Hydrolases
Escherichia coli
Ligands
Amino Acids
C-terminal processing peptidase
DegP protease
In Vitro Techniques
interstitial retinol-binding protein

All Science Journal Classification (ASJC) codes

  • General

Cite this

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abstract = "An Escherichia coli protease designated Tsp (tail-specific protease) has been purified, and its gene has been cloned and sequenced. Tsp specifically degrades a variant of the N-terminal domain of A represser in which the five C-terminal residues, which are polar in wild type, have been replaced by nonpolar residues. This substrate specificity in vitro parallels the previously reported selective degradation in vivo of N-terminal-domain variants with nonpolar C-terminal residues. The gene sequence and N-terminal protein sequence of Tsp predict a protein of 660 amino acids. The deduced protein sequence of Tsp shows no significant homology to known protease sequences but does show sequence similarity to the human and bovine interphotoreceptor retinoid-binding proteins, which bind hydrophobic ligands.",
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Tsp : A tail-specific protease that selectively degrades proteins with nonpolar C termini. / Silber, Karen R.; Keiler, Kenneth Charles; Sauer, Robert T.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 1, 01.01.1992, p. 295-299.

Research output: Contribution to journalArticle

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