ZapG (YhcB/DUF1043), a novel cell division protein in gamma-proteobacteria linking the Z-ring to septal peptidoglycan synthesis.

ZapG (YhcB/DUF1043), a novel cell division protein in gamma-proteobacteria linking the Z-ring to septal peptidoglycan synthesis.
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DOI:
10.1016/j.jbc.2021.100700
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发表时间:
2021-01
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
Uetz P
Uetz P
中科院分区:
其他
文献类型:
--
作者:
Mehla J;Liechti G;Morgenstein RM;Caufield JH;Hosseinnia A;Gagarinova A;Phanse S;Goodacre N;Brockett M;Sakhawalkar N;Babu M;Xiao R;Montelione GT;Vorobiev S;den Blaauwen T;Hunt JF;Uetz P

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YhcB是一种在γ-变形菌中保守的知之甚少的蛋白质,含有一个功能未知的结构域(DUF 1043)和一个N-末端跨膜结构域。在这里,我们使用了一个综合的方法,包括X射线晶体学,遗传学和分子生物学研究的功能和结构的YhcB。大肠杆菌yhcB KO菌株在45 °C下不生长,并且即使在稳定期也对细胞壁作用抗生素过敏。yhcB的缺失会导致基因重排、异常FtsZ环形成和异常隔发育。Z形环对于隔膜的定位和细胞分裂的启动是必不可少的。我们发现YhcB与分裂体的蛋白质相互作用(例如,FtsI,FtsQ)和延长酶体(例如,RodZ、RodA)。这些相互作用中的七种在鼠疫耶尔森氏菌和/或霍乱弧菌中也是保守的。此外,我们映射的氨基酸残基可能参与YhcB与FtsI和RodZ的相互作用。杜克雷嗜血杆菌YhcB胞质结构域的2.8 nm晶体结构显示出独特的四聚体α-螺旋卷曲螺旋结构,可能参与将Z环连接至间隔肽聚糖合成复合物。总之,YhcB是一种保守的和条件必需的蛋白质,在细胞分裂中发挥作用,从而影响包膜生物发生。基于这些发现,我们建议将YhcB重命名为ZapG(Z环相关蛋白G)。这项研究将作为未来研究这个蛋白质家族以及细胞如何从指数生存过渡到稳定生存的起点。
YhcB, a poorly understood protein conserved across gamma-proteobacteria, contains a domain of unknown function (DUF1043) and an N-terminal transmembrane domain. Here, we used an integrated approach including X-ray crystallography, genetics, and molecular biology to investigate the function and structure of YhcB. The Escherichia coli yhcB KO strain does not grow at 45 °C and is hypersensitive to cell wall–acting antibiotics, even in the stationary phase. The deletion of yhcB leads to filamentation, abnormal FtsZ ring formation, and aberrant septum development. The Z-ring is essential for the positioning of the septa and the initiation of cell division. We found that YhcB interacts with proteins of the divisome (e.g., FtsI, FtsQ) and elongasome (e.g., RodZ, RodA). Seven of these interactions are also conserved in Yersinia pestis and/or Vibrio cholerae. Furthermore, we mapped the amino acid residues likely involved in the interactions of YhcB with FtsI and RodZ. The 2.8 Å crystal structure of the cytosolic domain of Haemophilus ducreyi YhcB shows a unique tetrameric α-helical coiled-coil structure likely to be involved in linking the Z-ring to the septal peptidoglycan-synthesizing complexes. In summary, YhcB is a conserved and conditionally essential protein that plays a role in cell division and consequently affects envelope biogenesis. Based on these findings, we propose to rename YhcB to ZapG (Z-ring-associated protein G). This study will serve as a starting point for future studies on this protein family and on how cells transit from exponential to stationary survival.
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