Cloning and sequence analysis of pituitary cDNA encoding the beta-subunit of Xenopus proteasome.
The proteasome is a multicatalytic proteinase composed of a number of non-identical subunits. A Xenopus pituitary cDNA was isolated and found to code for the beta-subunit of proteasome. The amino acid sequence deduced from the open reading frame consisted of 215 amino acid residues with a calculated molecular weight of 23,979. A comparative structural analysis indicated that the proteasome subunits can be divided into two groups with the same evolutionary origin. One group consists of subunits with an N-terminally blocked residue and includes components C2, C3, C8 and C9, while the second group of non-blocked proteins includes component C5 and the beta-subunit.
Department of Animal Physiology, University of Nijmegen, The Netherlands.
M C
MC
van Riel
G J
GJ
Martens
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics*; D004247:DNA; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry / Q000235:genetics*; D010902:Pituitary Gland / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex; D016415:Sequence Alignment; D014982:Xenopus laevis
D009097:Multienzyme Complexes; D004247:DNA; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex