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Identification and architecture of a putative secretion tube across mycobacterial outer envelope
Tuberculosis-causing mycobacteria have thick cell-wall and capsule layers that are formed from complex structures. Protein secretion across these barriers depends on a specialized protein secretion system, but none has been reported. We show that Mycobacterium tuberculosis Rv3705c and its homologous...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8378821/ https://www.ncbi.nlm.nih.gov/pubmed/34417177 http://dx.doi.org/10.1126/sciadv.abg5656 |
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author | Cai, Xiaoying Liu, Lei Qiu, Chunhong Wen, Chongzheng He, Yao Cui, Yanxiang Li, Siyu Zhang, Xuan Zhang, Longhua Tian, Changlin Bi, Lijun Zhou, Z. Hong Gong, Weimin |
author_facet | Cai, Xiaoying Liu, Lei Qiu, Chunhong Wen, Chongzheng He, Yao Cui, Yanxiang Li, Siyu Zhang, Xuan Zhang, Longhua Tian, Changlin Bi, Lijun Zhou, Z. Hong Gong, Weimin |
author_sort | Cai, Xiaoying |
collection | PubMed |
description | Tuberculosis-causing mycobacteria have thick cell-wall and capsule layers that are formed from complex structures. Protein secretion across these barriers depends on a specialized protein secretion system, but none has been reported. We show that Mycobacterium tuberculosis Rv3705c and its homologous MSMEG_6251 in Mycobacterium smegmatis are tube-forming proteins in the mycobacterial envelope (TiME). Crystallographic and cryo-EM structures of these two proteins show that both proteins form rotationally symmetric rings. Two layers of TiME rings pack together in a tail-to-tail manner into a ring-shaped complex, which, in turn, stacks together to form tubes. M. smegmatis TiME was detected mainly in the cell wall and capsule. Knocking out the TiME gene markedly decreased the amount of secreted protein in the M. smegmatis culture medium, and expression of this gene in knocked-out strain partially restored the level of secreted protein. Our structure and functional data thus suggest that TiME forms a protein transport tube across the mycobacterial outer envelope. |
format | Online Article Text |
id | pubmed-8378821 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-83788212021-08-30 Identification and architecture of a putative secretion tube across mycobacterial outer envelope Cai, Xiaoying Liu, Lei Qiu, Chunhong Wen, Chongzheng He, Yao Cui, Yanxiang Li, Siyu Zhang, Xuan Zhang, Longhua Tian, Changlin Bi, Lijun Zhou, Z. Hong Gong, Weimin Sci Adv Research Articles Tuberculosis-causing mycobacteria have thick cell-wall and capsule layers that are formed from complex structures. Protein secretion across these barriers depends on a specialized protein secretion system, but none has been reported. We show that Mycobacterium tuberculosis Rv3705c and its homologous MSMEG_6251 in Mycobacterium smegmatis are tube-forming proteins in the mycobacterial envelope (TiME). Crystallographic and cryo-EM structures of these two proteins show that both proteins form rotationally symmetric rings. Two layers of TiME rings pack together in a tail-to-tail manner into a ring-shaped complex, which, in turn, stacks together to form tubes. M. smegmatis TiME was detected mainly in the cell wall and capsule. Knocking out the TiME gene markedly decreased the amount of secreted protein in the M. smegmatis culture medium, and expression of this gene in knocked-out strain partially restored the level of secreted protein. Our structure and functional data thus suggest that TiME forms a protein transport tube across the mycobacterial outer envelope. American Association for the Advancement of Science 2021-08-20 /pmc/articles/PMC8378821/ /pubmed/34417177 http://dx.doi.org/10.1126/sciadv.abg5656 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Cai, Xiaoying Liu, Lei Qiu, Chunhong Wen, Chongzheng He, Yao Cui, Yanxiang Li, Siyu Zhang, Xuan Zhang, Longhua Tian, Changlin Bi, Lijun Zhou, Z. Hong Gong, Weimin Identification and architecture of a putative secretion tube across mycobacterial outer envelope |
title | Identification and architecture of a putative secretion tube across mycobacterial outer envelope |
title_full | Identification and architecture of a putative secretion tube across mycobacterial outer envelope |
title_fullStr | Identification and architecture of a putative secretion tube across mycobacterial outer envelope |
title_full_unstemmed | Identification and architecture of a putative secretion tube across mycobacterial outer envelope |
title_short | Identification and architecture of a putative secretion tube across mycobacterial outer envelope |
title_sort | identification and architecture of a putative secretion tube across mycobacterial outer envelope |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8378821/ https://www.ncbi.nlm.nih.gov/pubmed/34417177 http://dx.doi.org/10.1126/sciadv.abg5656 |
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