DrpB (YedR) Is a Nonessential Cell Division Protein in Escherichia coli.
DrpB (YedR) Is a Nonessential Cell Division Protein in Escherichia coli.
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DrpB（YedR）是大肠杆菌中一种非必需的细胞分裂蛋白。
DOI：
10.1128/jb.00284-20
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发表时间：
2020-11-04
影响因子：
3.2
通讯作者：
Weiss DS
中科院分区：
文献类型：
--
作者：
Yahashiri A;Babor JT;Anwar AL;Bezy RP;Piette EW;Arends SJR;Müh U;Steffen MR;Cline JM;Stanek DN;Lister SD;Swanson SM;Weiss DS
要彻底了解细菌细胞分裂，需要鉴定和表征参与这一过程的所有蛋白质。DrpB的发现使我们在E.杆菌我们报告说，小大肠杆菌膜蛋白DrpB（以前的YedR）参与细胞分裂。我们在筛选ΔftsEX突变的多拷贝抑制子时发现了DrpB，当细胞接种在低离子强度培养基（如不含NaCl的溶原性肉汤）上时，该突变可阻止分裂体组装。DrpB的表征揭示了（i）翻译起始于标注为密码子22的ATG而不是标注为密码子1的GTG，（ii）当细胞在低离子强度的培养基中生长时，DrpB定位于隔环，但在高离子强度的培养基中定位大大减少，（iii）在ΔftsEX突变体背景中过量产生DrpB改善了隔肽聚糖合酶FtsI的募集，（iv）ΔdrpB突变体的分裂非常正常，而ΔdrpB ΔdedD双突变体的分裂和活力缺陷很强，但只在高离子强度的介质中存在;（v）在E.大肠杆菌和一些密切相关的肠道细菌，但不是在这组之外。总之，DrpB是一种保守性差的非必需分裂蛋白，其在次优条件下提高胞质分裂的效率。像DrpB这样的蛋白质很可能是细菌细胞分裂装置的一个普遍特征，但它们很容易被忽视，因为突变体缺乏明显的形状缺陷。要彻底了解细菌细胞分裂，需要鉴定和表征参与这一过程的所有蛋白质。DrpB的发现使我们在E.杆菌
A thorough understanding of bacterial cell division requires identifying and characterizing all of the proteins that participate in this process. Our discovery of DrpB brings us one step closer to this goal in E. coli. We report that the small Escherichia coli membrane protein DrpB (formerly YedR) is involved in cell division. We discovered DrpB in a screen for multicopy suppressors of a ΔftsEX mutation that prevents divisome assembly when cells are plated on low ionic strength medium, such as lysogeny broth without NaCl. Characterization of DrpB revealed that (i) translation initiates at an ATG annotated as codon 22 rather than the GTG annotated as codon 1, (ii) DrpB localizes to the septal ring when cells are grown in medium of low ionic strength but localization is greatly reduced in medium of high ionic strength, (iii) overproduction of DrpB in a ΔftsEX mutant background improves recruitment of the septal peptidoglycan synthase FtsI, implying multicopy suppression works by rescuing septal ring assembly, (iv) a ΔdrpB mutant divides quite normally, but a ΔdrpB ΔdedD double mutant has a strong division and viability defect, albeit only in medium of high ionic strength, and (v) DrpB homologs are found in E. coli and a few closely related enteric bacteria, but not outside this group. In sum, DrpB is a poorly conserved nonessential division protein that improves the efficiency of cytokinesis under suboptimal conditions. Proteins like DrpB are likely to be a widespread feature of the bacterial cell division apparatus, but they are easily overlooked because mutants lack obvious shape defects. IMPORTANCE A thorough understanding of bacterial cell division requires identifying and characterizing all of the proteins that participate in this process. Our discovery of DrpB brings us one step closer to this goal in E. coli.