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EnglishA full-length 515 base pairs cDNA for cytochrome c oxidase subunit V of D. discoideum was isolated from a lambda gt11 expression library. The encoded polypeptide, whose identity was confirmed by partial protein sequencing, is 119 amino acids long (Mr = 13,352) and does not contain a cleavable presequence. The protein, which is homologous to human subunit Vb and yeast subunit IV, exhibits the highest degree of sequence conservation found among nuclear-encoded subunits of cytochrome c oxidase from distantly related organisms. All the invariant residues are clustered in two regions of the C-terminus which include the putative amino acids involved in the coordination of the Zn ion tightly associated to eukaryotic oxidase.
| Titolo: | THE MOST CONSERVED NUCLEAR-ENCODED POLYPEPTIDE OF CYTOCHROME-C- OXIDASE IS THE PUTATIVE ZINC-BINDING SUBUNIT - PRIMARY STRUCTURE OF SUBUNIT-V FROM THE SLIME-MOLD DICTYOSTELIUM- DISCOIDEUM |
| Autori: | |
| Data di pubblicazione: | 1991 |
| Rivista: | |
| Abstract: | A full-length 515 base pairs cDNA for cytochrome c oxidase subunit V of D. discoideum was isolated from a lambda gt11 expression library. The encoded polypeptide, whose identity was confirmed by partial protein sequencing, is 119 amino acids long (Mr = 13,352) and does not contain a cleavable presequence. The protein, which is homologous to human subunit Vb and yeast subunit IV, exhibits the highest degree of sequence conservation found among nuclear-encoded subunits of cytochrome c oxidase from distantly related organisms. All the invariant residues are clustered in two regions of the C-terminus which include the putative amino acids involved in the coordination of the Zn ion tightly associated to eukaryotic oxidase. |
| Handle: | http://hdl.handle.net/11577/2473474 |
| Appare nelle tipologie: | 01.01 - Articolo in rivista |
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