GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape in Agrobacterium tumefaciens
| Autor: | Romain Grangeon, John R. Zupan, J. S. Robalino-Espinosa, N. Garnica, Patricia Zambryski |
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| Přispěvatelé: | Structural Biology |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Morphology
apolipoprotein Agrobacterium Cell Cycle Proteins Ring (chemistry) chemistry.chemical_compound Rod-shape Bacterial Proteins SDG 14 - Life Below Water rod-shape morphology GROWTH POLE RING protein FtsZ Cell Shape bacterial polar growth Multidisciplinary biology Chemistry fungi Agrobacterium tumefaciens Biological Sciences biology.organism_classification Apolipoprotein Transmembrane domain Cytoplasm biology.protein Biophysics Bacterial polar growth Generic health relevance Peptidoglycan FtsA Cell envelope Cell Division |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America, 166(22), 10962-10967. National Acad Sciences Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 22 Zupan, J R, Grangeon, R, Robalino-Espinosa, J S, Garnica, N & Zambryski, P 2019, ' GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape in Agrobacterium tumefaciens ', Proceedings of the National Academy of Sciences of the United States of America, vol. 166, no. 22, pp. 10962-10967 . https://doi.org/10.1073/pnas.1905900116 |
| ISSN: | 0027-8424 |
| DOI: | 10.1073/pnas.1905900116 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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