Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues
| Autor: | Hans G. Nothwang, Akira Ichihara, Tomohiro Tamura, Keiji Tanaka |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Proteasome Endopeptidase Complex
DNA Complementary Molecular Sequence Data Restriction Mapping Biophysics Sequence alignment Biochemistry chemistry.chemical_compound Multienzyme Complexes Structural Biology Consensus Sequence Genetics Consensus sequence Animals Nucleotide Amino Acid Sequence Cloning Molecular Binding site Peptide sequence chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid biology Active site Amino acid Molecular Weight Cysteine Endopeptidases Solubility chemistry Multigene Family biology.protein Cattle Sequence Alignment DNA |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1219:361-368 |
| ISSN: | 0167-4781 |
| DOI: | 10.1016/0167-4781(94)90060-4 |
| Popis: | 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 29192, 22836 and 22931, respectively. Sequence comparison showed that all three proteins belong to the β-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. |
| Databáze: | OpenAIRE |
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