Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling

Bacteria adjust the expression of some of their metabolic enzymes through metabolite-sensing ribosome nascent chain complexes. Here the authors present a cryo-EM structure of an E. coli ribosome stalled during translation of the TnaC leader peptide and propose a model for L-Trp dependent ribosome st...

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Autores principales:	Anne-Xander van der Stel, Emily R. Gordon, Arnab Sengupta, Allyson K. Martínez, Dorota Klepacki, Thomas N. Perry, Alba Herrero del Valle, Nora Vázquez-Laslop, Matthew S. Sachs, Luis R. Cruz-Vera, C. Axel Innis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/99346a81e0d045cab5ff4b2e4b54f7d9
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spelling	oai:doaj.org-article:99346a81e0d045cab5ff4b2e4b54f7d92021-12-02T17:42:11ZStructural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling10.1038/s41467-021-25663-82041-1723https://doaj.org/article/99346a81e0d045cab5ff4b2e4b54f7d92021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25663-8https://doaj.org/toc/2041-1723Bacteria adjust the expression of some of their metabolic enzymes through metabolite-sensing ribosome nascent chain complexes. Here the authors present a cryo-EM structure of an E. coli ribosome stalled during translation of the TnaC leader peptide and propose a model for L-Trp dependent ribosome stalling where L-Trp competes with release factor 2 for binding to the TnaC-ribosome complex.Anne-Xander van der StelEmily R. GordonArnab SenguptaAllyson K. MartínezDorota KlepackiThomas N. PerryAlba Herrero del ValleNora Vázquez-LaslopMatthew S. SachsLuis R. Cruz-VeraC. Axel InnisNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Anne-Xander van der Stel Emily R. Gordon Arnab Sengupta Allyson K. Martínez Dorota Klepacki Thomas N. Perry Alba Herrero del Valle Nora Vázquez-Laslop Matthew S. Sachs Luis R. Cruz-Vera C. Axel Innis Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling
description	Bacteria adjust the expression of some of their metabolic enzymes through metabolite-sensing ribosome nascent chain complexes. Here the authors present a cryo-EM structure of an E. coli ribosome stalled during translation of the TnaC leader peptide and propose a model for L-Trp dependent ribosome stalling where L-Trp competes with release factor 2 for binding to the TnaC-ribosome complex.
format	article
author	Anne-Xander van der Stel Emily R. Gordon Arnab Sengupta Allyson K. Martínez Dorota Klepacki Thomas N. Perry Alba Herrero del Valle Nora Vázquez-Laslop Matthew S. Sachs Luis R. Cruz-Vera C. Axel Innis
author_facet	Anne-Xander van der Stel Emily R. Gordon Arnab Sengupta Allyson K. Martínez Dorota Klepacki Thomas N. Perry Alba Herrero del Valle Nora Vázquez-Laslop Matthew S. Sachs Luis R. Cruz-Vera C. Axel Innis
author_sort	Anne-Xander van der Stel
title	Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling
title_short	Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling
title_full	Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling
title_fullStr	Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling
title_full_unstemmed	Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling
title_sort	structural basis for the tryptophan sensitivity of tnac-mediated ribosome stalling
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/99346a81e0d045cab5ff4b2e4b54f7d9
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_version_	1718379659873222656

Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling

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