Existence of a molecular ruler in proteasomes suggested by analysis of degradation products
Open Access
- 1 August 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 349 (2) , 205-209
- https://doi.org/10.1016/0014-5793(94)00665-2
Abstract
Analysis of the degradation products from two proteins, the insulin B‐chain and human hemoglobin, generated by archaebacterial Thermoplasma acidophilum 20 S proteasomes, revealed an unexpectedly broad specificity. In spite of the vast number of different peptides found, they fell into a rather narrow size range. This suggests that a molecular ruler exists which determines the length of the cleavage products.Keywords
This publication has 32 references indexed in Scilit:
- Structural Features of the 26 S Proteasome ComplexJournal of Molecular Biology, 1993
- Preliminary X-ray Crystallographic Study of the Proteasome from Thermoplasma acidophilumJournal of Molecular Biology, 1993
- Thermoplasma acidophilum proteasomes degrade partially unfolded and ubiquitin‐associated proteinsFEBS Letters, 1993
- Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acidsBiochemistry, 1993
- Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coliFEBS Letters, 1992
- The three‐dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tiltingFEBS Letters, 1991
- Degradation of oxidized insulin B chain by the multiproteinase complex macropain (proteasome)Biochemistry, 1991
- The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteriaFEBS Letters, 1989
- Electron microscopy and image analysis of the multicatalytic proteinaseFEBS Letters, 1988
- Identification of three high molecular mass cysteine proteinases from rat skeletal muscleFEBS Letters, 1983