期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 85, 期 2, 页码 297-306出版社
OXFORD UNIV PRESS
DOI: 10.1093/bbb/zbaa037
关键词
YjgF; YER057c; UK114; YabJ; X-ray crystallographic structure; gain-of-function mutation; Bacillus subtilis
类别
资金
- Ministry of Agriculture, Forestry, and Fisheries
- UNU-Kirin fellowship program
The study revealed that the dominant allele of yabJ gene caused by a single amino acid mutation leads to changes in B. subtilis production, and the structural change may be related to the inversion of the fifth beta-strand, affecting its ligand-binding capability.
Bacillus subtilis YabJ protein belongs to the highly conserved YjgF/YER057c/UK114 family, which has a homotrimeric quaternary structure. The dominant allele of yabJ gene that is caused by a single amino acid mutation of Ser103Phe enables poly-gamma-glutamic acid (gamma PGA) production of B. subtilis under conditions where the cell-density signal transduction was disturbed by the loss of DegQ function. X-ray crystallography of recombinant proteins revealed that unlike the homotrimeric wild-type YabJ, the mutant YabJ(Ser103Phe) had a homotetrameric quaternary structure, and the structural change appeared to be triggered by an inversion of the fifth beta-strand. The YabJ homotetramer has a hole that is highly accessible, penetrating through the tetramer, and 2 surface concaves as potential ligand-binding sites. Western blot analyses revealed that the conformational change was also induced in vivo by the Ser103Phe mutation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据