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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
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.
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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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