Structure and inherent properties of the bacteriophage lambda head shell. VII. Molecular design of the form-determining major capsid protein.
Structure and inherent properties of the bacteriophage lambda head shell. VII. Molecular design of the form-determining major capsid protein.
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噬菌体 lambda 头壳的结构和固有特性。
DOI:
10.1016/s0022-2836(05)80211-6
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发表时间:
1983
影响因子:
5.6
通讯作者:
H. Kobayashi
中科院分区:
文献类型:
--
作者:
I. Katsura;H. Kobayashi
Some mutations in the major capsid protein (gpE) ofλphage can alter the size and shape of the head shell or block the pathway of head maturation. Previous studies on the classification of such mutants showed that there are at least five functional sites on the gpE molecule. In this study, we determined the amino acid exchanges by DNA sequencing to elucidate the molecular design of the form-determining multifunctional protein gpE. In addition, we characterized the mutated gpE molecules by two-dimensional gel electrophoresis and studied suppression patterns of amber mutants at 43 amino acid residues.Those mutations map at 19 amino acid residues at 22 bases, which are located in three regions, 40 to 91, 222 to 246, and 284 to 324 of the 341 amino acid residues of gpE. These regions seem to be important in the activity of gpE, since amber mutations in these regions are suppressed on the average by less species of suppressors than those outside these regions. The mutations having different phenotypes are not segregated from each other, while some mutations having the same phenotype are separated far apart in the primary structure. This suggests that the functional sites were formed during evolution after the folding pattern of the ancestral gpE polypeptide chain had been established. Many of the mutations are located at serine, glycine and proline residues in predictedβ-turns.
影响因子:
3.4
作者:
S. Harrison
通讯作者:
S. Harrison
影响因子:
5.6
作者:
Tsui,L;Hendrix,RW
通讯作者:
Hendrix,RW
影响因子:
5.6
作者:
Rossmann,MG;Abad-Zapatero,C;Hermodson,MA;Erickson,JW
通讯作者:
Erickson,JW