Existence of a molecular ruler in proteasomes suggested by analysis of degradation products

FEBS Lett. 1994 Aug 1;349(2):205-9. doi: 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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism*
  • Hemoglobins / chemistry
  • Hemoglobins / metabolism
  • Humans
  • Insulin / chemistry
  • Insulin / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism*
  • Proteasome Endopeptidase Complex
  • Thermoplasma / enzymology*

Substances

  • Hemoglobins
  • Insulin
  • Multienzyme Complexes
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex