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FtsN非必需N端在分裂体组装中的作用。

Role for the nonessential N terminus of FtsN in divisome assembly.

作者信息

Goehring Nathan W, Robichon Carine, Beckwith Jon

机构信息

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.

出版信息

J Bacteriol. 2007 Jan;189(2):646-9. doi: 10.1128/JB.00992-06. Epub 2006 Oct 27.

Abstract

FtsN, the last essential protein in the cell division localization hierarchy in Escherichia coli, has several peculiar characteristics, suggesting that it has a unique role in the division process despite the fact that it is conserved in only a subset of bacteria. In addition to suppressing temperature-sensitive mutations in ftsA, ftsK, ftsQ, and ftsI, overexpression of FtsN can compensate for a complete lack of FtsK in the cell. We examined the requirements for this phenomenon. We found that the N-terminal terminal region (cytoplasmic and transmembrane domains) is critical for suppression, while the C-terminal murein-binding domain is dispensable. Our results further suggest that FtsN and FtsK act cooperatively to stabilize the divisome.

摘要

FtsN是大肠杆菌细胞分裂定位层级中最后一个必需蛋白,它具有几个独特的特征,这表明尽管它仅在一部分细菌中保守,但在分裂过程中具有独特作用。除了抑制ftsA、ftsK、ftsQ和ftsI中的温度敏感突变外,FtsN的过表达可以弥补细胞中完全缺乏FtsK的情况。我们研究了这种现象的条件。我们发现N端区域(细胞质和跨膜结构域)对于抑制至关重要,而C端胞壁质结合结构域则是可有可无的。我们的结果进一步表明,FtsN和FtsK协同作用以稳定分裂体。

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