LOCATION OF AMINO ACID EXCHANGES IN CHEMICALLY EVOKED MUTANTS OF TOBACCO MOSAIC VIRUS.
LOCATION OF AMINO ACID EXCHANGES IN CHEMICALLY EVOKED MUTANTS OF TOBACCO MOSAIC VIRUS.
复制标题
烟草花叶病毒化学诱发突变体中氨基酸交换的位置。
DOI:
10.1021/bi00897a028
复制
发表时间:
1964
期刊:
影响因子:
2.9
通讯作者:
H. Fraenkel
中科院分区:
文献类型:
--
作者:
G. Funatsu;H. Fraenkel
Through the use of limited digestion by Nagarse the big N-terminal tryptic peptide of tobacco mosaic virus protein was fragmented and the amino acid exchanges occurring in this peptide in several mutants were localized. Enzymatic methodsand partial acid degradation made it possible to localize exchanges also inother parts of the molecule. Of about forty-four ex-changes observed and localized in our laboratory twenty-four were in the N-terminal and C-terminal 25-residue segments. No mutant or natural strain was found by us or elsewhere which differed from the wild type in the segment comprised by residues 108-122, andvery few ex-changes have been observed in the preceding 8-residue segment. The total number of dif-ferent exchanges observed by us were thirteen, four of which recurred frequently and usually involved the same amino acid residues in the peptide chain. The mechanism leading to ex-changes in terms of known codons was discussed.Studies on the protein structure of chemically evoked mutants of tobacco mosaic virus (TMV) 1 have been carried out over the past years in our laboratory and at the Max Planck Instituí für Biologie at Tübingen (Tsugita and Fraenkel-Conrat, 1962; Tsugita, 1962a; Wittmann, 1962), in the hope that these would supply definite information about the genetic code. In both laboratories many of the mutants studied showed re-placements of one or two and more rarely three amino acid residues, while many others showed no exchanges. Though these exchanges were scattered over the entire sequence, they occurred frequently in peptide 12 (Tsugita, 1962a). The localization of these amino acid exchanges in peptide 1 was not attempted because of technical difficulties related to its size (forty-one amino acids) and to the lability of some of its peptide bonds. In this paper we present data on the location of these amino acid replacements in ten strains previously re-ported and in nine new strains.