Decelerated degradation of short peptides by the 20s proteasome

Dolenc, I.; Seemüller, E.; Baumeister, W.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Decelerated degradation of short peptides by the 20s proteasome

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Dolenc, I., Seemüller, E., & Baumeister, W. (1998). Decelerated degradation of short peptides by the 20s proteasome. FEBS Letters, 434(3), 357-361.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-71F5-B

Abstract

Based on a twelve residue master peptide comprising all five specific cleavage sites defined for the proteasome, a set of variant peptides was generated in order to probe specificity and to elucidate the mechanism which determines product size. It is shown that the rate of degradation by the 20S proteasome from Thermoplasma acidophilum depends critically on the length of the peptide substrate. Peptides of 14 residues and longer are degraded much faster than shorter peptides although the sites of cleavage remain unchanged. The decelerated degradation of peptides shorter than 14 residues explains the accumulation of products with an average length of seven to nine residues, (C) 1998 Federation of European Biochemical Societies. [References: 17]