Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes

Abtract Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs...

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Autores principales:	Pedro Bule, Victor D. Alves, Vered Israeli-Ruimy, Ana L. Carvalho, Luís M. A. Ferreira, Steven P. Smith, Harry J. Gilbert, Shabir Najmudin, Edward A. Bayer, Carlos M. G. A. Fontes
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f3fb9c1f467240e492c65c6aa18d7234
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spelling	oai:doaj.org-article:f3fb9c1f467240e492c65c6aa18d72342021-12-02T11:40:13ZAssembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes10.1038/s41598-017-00919-w2045-2322https://doaj.org/article/f3fb9c1f467240e492c65c6aa18d72342017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00919-whttps://doaj.org/toc/2045-2322Abtract Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs appended to cellulosomal enzymes generally present two similar Coh-binding interfaces supporting a dual-binding mode, which may confer increased positional adjustment of the different complex components. Ruminococcus flavefaciens’ cellulosome is assembled from a repertoire of 223 Doc-containing proteins classified into 6 groups. Recent studies revealed that Docs of groups 3 and 6 are recruited to the cellulosome via a single-binding mode mechanism with an adaptor scaffoldin. To investigate the extent to which the single-binding mode contributes to the assembly of R. flavefaciens cellulosome, the structures of two group 1 Docs bound to Cohs of primary (ScaA) and adaptor (ScaB) scaffoldins were solved. The data revealed that group 1 Docs display a conserved mechanism of Coh recognition involving a single-binding mode. Therefore, in contrast to all cellulosomes described to date, the assembly of R. flavefaciens cellulosome involves single but not dual-binding mode Docs. Thus, this work reveals a novel mechanism of cellulosome assembly and challenges the ubiquitous implication of the dual-binding mode in the acquisition of cellulosome flexibility.Pedro BuleVictor D. AlvesVered Israeli-RuimyAna L. CarvalhoLuís M. A. FerreiraSteven P. SmithHarry J. GilbertShabir NajmudinEdward A. BayerCarlos M. G. A. FontesNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Pedro Bule Victor D. Alves Vered Israeli-Ruimy Ana L. Carvalho Luís M. A. Ferreira Steven P. Smith Harry J. Gilbert Shabir Najmudin Edward A. Bayer Carlos M. G. A. Fontes Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
description	Abtract Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs appended to cellulosomal enzymes generally present two similar Coh-binding interfaces supporting a dual-binding mode, which may confer increased positional adjustment of the different complex components. Ruminococcus flavefaciens’ cellulosome is assembled from a repertoire of 223 Doc-containing proteins classified into 6 groups. Recent studies revealed that Docs of groups 3 and 6 are recruited to the cellulosome via a single-binding mode mechanism with an adaptor scaffoldin. To investigate the extent to which the single-binding mode contributes to the assembly of R. flavefaciens cellulosome, the structures of two group 1 Docs bound to Cohs of primary (ScaA) and adaptor (ScaB) scaffoldins were solved. The data revealed that group 1 Docs display a conserved mechanism of Coh recognition involving a single-binding mode. Therefore, in contrast to all cellulosomes described to date, the assembly of R. flavefaciens cellulosome involves single but not dual-binding mode Docs. Thus, this work reveals a novel mechanism of cellulosome assembly and challenges the ubiquitous implication of the dual-binding mode in the acquisition of cellulosome flexibility.
format	article
author	Pedro Bule Victor D. Alves Vered Israeli-Ruimy Ana L. Carvalho Luís M. A. Ferreira Steven P. Smith Harry J. Gilbert Shabir Najmudin Edward A. Bayer Carlos M. G. A. Fontes
author_facet	Pedro Bule Victor D. Alves Vered Israeli-Ruimy Ana L. Carvalho Luís M. A. Ferreira Steven P. Smith Harry J. Gilbert Shabir Najmudin Edward A. Bayer Carlos M. G. A. Fontes
author_sort	Pedro Bule
title	Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
title_short	Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
title_full	Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
title_fullStr	Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
title_full_unstemmed	Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
title_sort	assembly of ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/f3fb9c1f467240e492c65c6aa18d7234
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Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes

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