Existence of a molecular ruler in proteasomes suggested by analysis of degradation products.
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.
Wenzel
T
T
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Eckerskorn
C
C
Lottspeich
F
F
Baumeister
W
W
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007328:Insulin / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D013822:Thermoplasma / Q000201:enzymology*
D006454:Hemoglobins; D007328:Insulin; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex