COTRANSLATIONAL PROCESSING AND PROTEIN-TURNOVER IN EUKARYOTIC CELLS
COTRANSLATIONAL PROCESSING AND PROTEIN-TURNOVER IN EUKARYOTIC CELLS
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DOI:
10.1021/bi00421a001
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发表时间:
1988-10-18
期刊:
影响因子:
2.9
通讯作者:
BRADSHAW, RA
中科院分区:
文献类型:
--
作者:
ARFIN, SM;BRADSHAW, RA
1987; Miller et al., 1987). Preliminary characterization of partially purified preparations of NAT and MAP suggests both enzymes are large, multimeric molecules. In addition, rat liver NAT preparations display extraordinary lability, as has been noted for NAT preparations from other sources(Driessen et al., 1985), that is only partially stabilized by EDTA and de-oxycholate (Yamada et al., 1987). The specificity of both enzymes has been surmised from an examination of the germane, directly determined structures found in the protein sequence data base (Persson et al., 1985; Driessen et al., 1985; Sherman et al., 1986) and by an exam-ination of a number of mutant proteins, primarily in yeast (Tsunasawa et al., 1985). These analyses, insofar as the data allow, suggest that MAP is inhibited by an adjacent charged or bulky residue (Burstein & Schechter, 1978; Sherman et al., 1986) and that iV “-acetyl groups tend to be added, with only a few exceptions, to terminal amino acids with relatively small side chains (Persson et al., 1985; Bloemendal, 1977). The primary specifying residue appears to be the penultimate amino acid (which becomes the N-terminal in instances where the initiator methionine is removed). However, computer analyses have also suggested that additional specifying influences may be found in regions as far as 40 residues from the amino terminus (Persson et al., 1985; Augen& Wold, 1986).