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GpsB在多个物种中与FtsZ相互作用,可能作为一种辅助性Z环锚定蛋白。

GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.

作者信息

Bhattacharya Dipanwita, King Asher, McKnight Lily, Horigian Pilar, Eswara Prahathees J

机构信息

Department of Molecular Biosciences, University of South Florida, Tampa, FL 33620.

Center for Antimicrobial Resistance, University of South Florida, Tampa, FL 33620.

出版信息

Mol Biol Cell. 2025 Jan 1;36(1):ar10. doi: 10.1091/mbc.E24-07-0302. Epub 2024 Nov 27.

DOI:10.1091/mbc.E24-07-0302
PMID:39602291
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11742113/
Abstract

Bacterial cytokinesis commences when a tubulin-like GTPase, FtsZ, forms a Z-ring to mark the division site. Synchronized movement of Z-ring filaments and peptidoglycan synthesis along the axis of division generates a division septum to separate the daughter cells. Thus, FtsZ needs to be linked to the peptidoglycan synthesis machinery. GpsB is a highly conserved protein among species of the Firmicutes phylum known to regulate peptidoglycan synthesis. Previously, we showed that GpsB directly binds to FtsZ by recognizing a signature sequence in its C-terminal tail (CTT) region. As the GpsB recognition sequence is also present in , we speculated that GpsB may interact with FtsZ in this organism. Earlier reports revealed that disruption of and or and is deleterious. Given that both FtsA and EzrA also target the CTT of FtsZ for interaction, we hypothesized that in the absence of other FtsZ partners, GpsB-FtsZ interaction may become apparent. Our data confirm that is the case, and reveal that GpsB interacts with FtsZ in multiple species and stimulates the GTPase activity of the latter. Moreover, it appears that GpsB may serve as an accessory Z-ring anchor such as when FtsA, one of the main anchors, is absent.

摘要

当一种微管蛋白样GTP酶FtsZ形成一个Z环以标记分裂位点时,细菌胞质分裂开始。Z环丝的同步移动以及肽聚糖沿着分裂轴的合成产生一个分裂隔膜以分隔子细胞。因此,FtsZ需要与肽聚糖合成机制相连接。GpsB是厚壁菌门物种中一种高度保守的蛋白质,已知其可调节肽聚糖合成。此前,我们表明GpsB通过识别FtsZ C末端尾巴(CTT)区域的一个特征序列直接与FtsZ结合。由于GpsB识别序列在[此处原文缺失相关信息]中也存在,我们推测GpsB可能在该生物体中与FtsZ相互作用。早期报告显示[此处原文缺失相关信息]和[此处原文缺失相关信息]或[此处原文缺失相关信息]和[此处原文缺失相关信息]的破坏是有害的。鉴于FtsA和EzrA也靶向FtsZ的CTT进行相互作用,我们假设在没有其他FtsZ伙伴的情况下,GpsB - FtsZ相互作用可能会变得明显。我们的数据证实情况确实如此,并揭示GpsB在多个物种中与FtsZ相互作用并刺激后者的GTP酶活性。此外,似乎GpsB可能作为一种辅助性Z环锚定物,例如当主要锚定物之一FtsA不存在时。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/556641f317bb/mbc-36-ar10-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/f4570456ed54/mbc-36-ar10-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/d022156933d3/mbc-36-ar10-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/2f0d0cbd1ee2/mbc-36-ar10-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/e3a719d36487/mbc-36-ar10-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/556641f317bb/mbc-36-ar10-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/f4570456ed54/mbc-36-ar10-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/d022156933d3/mbc-36-ar10-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/2f0d0cbd1ee2/mbc-36-ar10-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/e3a719d36487/mbc-36-ar10-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b74d/11742113/556641f317bb/mbc-36-ar10-g005.jpg

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