Insights into a type III cohesin-dockerin recognition interface from the cellulose-degrading bacterium Ruminococcus flavefaciens

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dc.authoridKarpol, Alon/0000-0001-8445-1877|Weinstein, Jonathan/0000-0001-7581-965X|Barak, Yoav/0000-0002-5063-0559
dc.authorwosidGul, Ozgur/A-7841-2011
dc.contributor.authorWeinstein, Jonathan Y.
dc.contributor.authorSlutzki, Michal
dc.contributor.authorKarpol, Alon
dc.contributor.authorBarak, Yoav
dc.contributor.authorGul, Ozgur
dc.contributor.authorLamed, Raphael
dc.contributor.authorBayer, Edward A.
dc.date.accessioned2024-07-18T20:40:02Z
dc.date.available2024-07-18T20:40:02Z
dc.date.issued2015
dc.departmentİstanbul Bilgi Üniversitesien_US
dc.description.abstractCellulosomes are large multicomponent cellulose-degrading assemblies found on the surfaces of cellulolytic microorganisms. Often containing hundreds of components, the self-assembly of cellulosomes is mediated by the ultra-high-affinity cohesin-dockerin interaction, which allows them to adopt the complex architectures necessary for degrading recalcitrant cellulose. Better understanding of how the cellulosome assembles and functions and what kinds of structures it adopts will further effort to develop industrial applications of cellulosome components, including their use in bioenergy production. Ruminococcus flavefaciens is a well-studied anaerobic cellulolytic bacteria found in the intestinal tracts of ruminants and other herbivores. Key to cellulosomal self-assembly in this bacterium is the dockerin ScaADoc, found on the non-catalytic structural subunit scaffoldin ScaA, which is responsible for assembling arrays of cellulose-degrading enzymes. This work expands on previous efforts by conducting a series of binding studies on ScaADoc constructs that contain mutations in their cohesin recognition interface, in order to identify which residues play important roles in binding. Molecular dynamics simulations were employed to gain insight into the structural basis for our findings. A specific residue pair in the first helix of ScaADoc, as well as a glutamate near the C-terminus, was identified to be essential for cohesin binding. By advancing our understanding of the cohesin binding of ScaADoc, this study serves as a foundation for future work to more fully understand the structural basis of cellulosome assembly in R. flavefaciens. Copyright (c) 2015 John Wiley & Sons, Ltd.en_US
dc.description.sponsorshipUnited States-Israel Binational Science Foundation (BSF), Jerusalem, Israel from the Israel Science Foundation (ISF) [1349]; Sidney E. Frank Foundation through the ISF [24/11]; United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel; Israeli Center of Research Excellence (I-CORE Center) [152/11]; Weizmann Institute of Science Alternative Energy Research Initiative (AERI) - Helmsley Foundationen_US
dc.description.sponsorshipThis research was supported by grants from the United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel, a grant (No. 1349) to EAB from the Israel Science Foundation (ISF) and a grant (No. 24/11) issued to RL by The Sidney E. Frank Foundation also through the ISF and by the United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel. Additional support was obtained from the establishment of an Israeli Center of Research Excellence (I-CORE Center No. 152/11, EAB) managed by the Israel Science Foundation, and by the Weizmann Institute of Science Alternative Energy Research Initiative (AERI), funded by the Helmsley Foundation. E.A.B. is the incumbent of The Maynard I. and Elaine Wishner Chair of Bio-organic Chemistry.en_US
dc.identifier.doi10.1002/jmr.2380
dc.identifier.endpage154en_US
dc.identifier.issn0952-3499
dc.identifier.issn1099-1352
dc.identifier.issue3en_US
dc.identifier.pmid25639797en_US
dc.identifier.scopus2-s2.0-84923332128en_US
dc.identifier.scopusqualityQ4en_US
dc.identifier.startpage148en_US
dc.identifier.urihttps://doi.org/10.1002/jmr.2380
dc.identifier.urihttps://hdl.handle.net/11411/6940
dc.identifier.volume28en_US
dc.identifier.wosWOS:000350260000004en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofJournal of Molecular Recognitionen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCellulosomeen_US
dc.subjectDockerinen_US
dc.subjectCohesinen_US
dc.subjectRuminococcus Flavefaciensen_US
dc.subjectClostridium Thermocellumen_US
dc.subjectCelluloseen_US
dc.subjectClostridium-Thermocellumen_US
dc.subjectHighly Efficienten_US
dc.subjectModuleen_US
dc.subjectGromacsen_US
dc.subjectSystemen_US
dc.subjectDomainen_US
dc.titleInsights into a type III cohesin-dockerin recognition interface from the cellulose-degrading bacterium Ruminococcus flavefaciensen_US
dc.typeArticleen_US

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