Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues.
Proteasomes play a major role in non-lysosomal pathways of protein turnover mediated by distinct multiple proteolytic activities. Identification of their active-site residues is important for elucidating their catalytic mechanisms. Here we report the nucleotide sequences of three human proteasomal subunits, HsN3, HsC7-I and HsC10-II, coding for proteins with 264, 201 and 205 amino acid residues with calculated molecular weights of 29,192, 22,836 and 22,931, respectively. Sequence comparison showed that all three proteins belong to the beta-type superfamily and that they are the human counterparts of subunits reported to participate in the peptidyl-glutamyl-peptide hydrolyzing, chymotrypsin-like and trypsin-like activity of this complex. Alignments of the putative catalytically active subunits of various species revealed several family-specifically conserved serinyl residues within highly conserved amino acid stretches. Based on localization and hydrophobicity, the roles of these amino acid residues as active site and substrate binding site candidates are discussed.
Nothwang
H G
HG
Institute for Enzyme Research, University of Tokushima, Japan.
Tamura
T
T
Tanaka
K
K
Ichihara
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D016384:Consensus Sequence; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D018076:DNA, Complementary / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000737:chemistry*; D005810:Multigene Family; D046988:Proteasome Endopeptidase Complex; D015183:Restriction Mapping; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012995:Solubility
D018076:DNA, Complementary; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex