globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1905900116
论文题名:
GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape in Agrobacterium tumefaciens
作者: Zupan J.R.; Grangeon R.; Robalino-Espinosa J.S.; Garnica N.; Zambryski P.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2019
卷: 166, 期:22
起始页码: 10962
结束页码: 10967
语种: 英语
英文关键词: Agrobacterium ; Apolipoprotein ; Bacterial polar growth ; GROWTH POLE RING protein ; Morphology ; Rod-shape
Scopus关键词: apolipoprotein ; bacterial protein ; growth pole ring protein ; lipid ; membrane protein ; peptidoglycan ; proline ; unclassified drug ; Agrobacterium tumefaciens ; alpha helix ; amino terminal sequence ; Article ; bacterial cell ; bacterial growth ; bacterial structures ; carboxy terminal sequence ; cell cycle ; cell membrane ; controlled study ; cytoplasm ; gene deletion ; nonhuman ; priority journal ; protein defect ; protein domain ; protein function ; protein localization ; protein structure ; Rhizobiales ; riboswitch ; sequence homology
英文摘要: Polar growth in Agrobacterium pirates and repurposes well-known bacterial cell cycle proteins, such as FtsZ, FtsA, PopZ, and PodJ. Here we identify a heretofore unknown protein that we name GROWTH POLE RING (GPR) due to its striking localization as a hexameric ring at the growth pole during polar growth. GPR also localizes at the midcell late in the cell cycle just before division, where it is then poised to be precisely localized at new growth poles in sibling cells. GPR is 2,115 aa long, with two N-terminal transmembrane domains placing the bulk of the protein in the cytoplasm, N- and C-terminal proline-rich disordered regions, and a large 1,700-aa central region of continuous α-helical domains. This latter region contains 12 predicted adjacent or overlapping apolipoprotein domains that may function to sequester lipids during polar growth. Stable genetic deletion or riboswitch-controlled depletion results in spherical cells that grow poorly; thus, GPR is essential for wild-type growth and morphology. As GPR has no predicted enzymatic domains and it forms a distinct 200-nm-diameter ring, we propose that GPR is a structural component of an organizing center for peptidoglycan and membrane syntheses critical for cell envelope formation during polar growth. GPR homologs are found in numerous Rhizobiales; thus, our results and proposed model are fundamental to understanding polar growth strategy in a variety of bacterial species. © 2019 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163555
Appears in Collections:气候变化与战略

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作者单位: Zupan, J.R., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, United States; Grangeon, R., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, United States; Robalino-Espinosa, J.S., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, United States, Department of Molecular Cell Biology, Vrije Universiteit Amsterdam, Amsterdam, 1081 HV, Netherlands; Garnica, N., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, United States; Zambryski, P., Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, United States

Recommended Citation:
Zupan J.R.,Grangeon R.,Robalino-Espinosa J.S.,et al. GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape in Agrobacterium tumefaciens[J]. Proceedings of the National Academy of Sciences of the United States of America,2019-01-01,166(22)
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