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C-terminal specific protein degradation: Activity and substrate specificity of the Tsp protease

Typearticle
DateProtein Science, 4:1507-1515
AuthorsKENNETH C. KEILER, KAREN R .  SILBER, KEVIN M.  DOWNARD, IOANNIS A .  PAPAYANNOPOULOS, KLAUS BIEMANN, AND  ROBERT  T.  SAUER
Year1994

The activity of Tsp,  a periplasmic endoprotease of Escherichia coli, has been characterized by assaying the cleavage of  protein and peptide substrates, determining the cleavage  sites  in several substrates, and investigating the kinetics of the cleavage reaction. Tsp efficiently cleaves substrates that have apolar residues and a free a-carboxylate at  the C-terminus. Tsp cleaves its substrates at a discrete number of sites but with rather  broad  primary sequence specificity. In  addition to preferences  for residues at  the C-terminus and cleavage sites, Tsp displays a preference  for substrates that  are not  stably  folded:  unstable  variants of Arc repressor are better  substrates than a hyperstable
mutant,  and a  peptide with little stable structure is cleaved more efficiently than a  protein  substrate. These data are consistent with a  model in which Tsp cleavage of  a  protein substrate involves binding to  the C-terminal  tail of the substrate,  transient denaturation of the  substrate,  and then recognition and hydrolysis of specific peptide bonds.

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