ArticleJournal of bacteriology2004
ScaC, an adaptor protein carrying a novel cohesin that expands the dockerin-binding repertoire of the Ruminococcus flavefaciens 17 cellulosome.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 63 citations in OpenAlex.
- A genomic analysis reveals the diversity of cellulosome displaying bacteria.Frontiers in microbiology · 2024Article
- Cellulosomes: Highly Efficient Cellulolytic Complexes.Sub-cellular biochemistry · 2021Review
- Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction.Scientific reports · 2018Article
- Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes.Scientific reports · 2017Article
- Complexity of the Ruminococcus flavefaciens FD-1 cellulosome reflects an expansion of family-related protein-protein interactions.Scientific reports · 2017Article
- Cellulosomes: bacterial nanomachines for dismantling plant polysaccharides.Nature reviews. Microbiology · 2017Review
- Broad phylogeny and functionality of cellulosomal components in the bovine rumen microbiome.Environmental microbiology · 2017Article
- Single Binding Mode Integration of Hemicellulose-degrading Enzymes via Adaptor Scaffoldins in Ruminococcus flavefaciens Cellulosome.The Journal of biological chemistry · 2016Article
- Adaptor Scaffoldins: An Original Strategy for Extended Designer Cellulosomes, Inspired from Nature.mBio · 2016Article
- Overexpression, crystallization and preliminary X-ray characterization of Ruminococcus flavefaciens scaffoldin C cohesin in complex with a dockerin from an uncharacterized CBM-containing protein.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Rumen cellulosomics: divergent fiber-degrading strategies revealed by comparative genome-wide analysis of six ruminococcal strains.PloS one · 2014Article
- A synthetic biology approach for evaluating the functional contribution of designer cellulosome components to deconstruction of cellulosic substrates.Biotechnology for biofuels · 2013Article
- Atypical cohesin-dockerin complex responsible for cell surface attachment of cellulosomal components: binding fidelity, promiscuity, and structural buttresses.The Journal of biological chemistry · 2013Article
- Expression of cellulosome components and type IV pili within the extracellular proteome of Ruminococcus flavefaciens 007.PloS one · 2013Article
- Ruminococcus faecis sp. nov., isolated from human faeces.Journal of microbiology (Seoul, Korea) · 2011Article
- Article
- Abundance and diversity of dockerin-containing proteins in the fiber-degrading rumen bacterium, Ruminococcus flavefaciens FD-1.PloS one · 2010Article
- Diversity and strain specificity of plant cell wall degrading enzymes revealed by the draft genome of Ruminococcus flavefaciens FD-1.PloS one · 2009Article
- Noncellulosomal cohesin- and dockerin-like modules in the three domains of life.FEMS microbiology letters · 2009Review
- Preliminary X-ray characterization of a novel type of anchoring cohesin from the cellulosome of Ruminococcus flavefaciens.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new gene, designated scaC and encoding a protein carrying a single cohesin, was identified in the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 as part of a gene cluster that also codes for the cellulosome structural components ScaA and ScaB. Phylogenetic analysis showed that the sequence of the ScaC cohesin is distinct from the sequences of other cohesins, including the sequences of R. flavefaciens ScaA and ScaB. The scaC gene product also includes at its C terminus a dockerin module that closely resembles those found in R. flavefaciens enzymes that bind to the cohesins of the primary ScaA scaffoldin. The putative cohesin domain and the C-terminal dockerin module were cloned and overexpressed in Escherichia coli as His(6)-tagged products (ScaC-Coh and ScaC-Doc, respectively). Affinity probing of protein extracts of R. flavefaciens 17 separated in one-dimensional and two-dimensional gels with recombinant cohesins from ScaC and ScaA revealed that two distinct subsets of native proteins interact with ScaC-Coh and ScaA-Coh. Furthermore, ScaC-Coh failed to interact with the recombinant dockerin module from the enzyme EndB that is recognized by ScaA cohesins. On the other hand, ScaC-Doc was shown to interact specifically with the recombinant cohesin domain from ScaA, and the ScaA-Coh probe was shown to interact with a native 29-kDa protein spot identified as ScaC by matrix-assisted laser desorption ionization-time of flight mass spectrometry. These results suggest that ScaC plays the role of an adaptor scaffoldin that is bound to ScaA via the ScaC dockerin module, which, via the distinctive ScaC cohesin, expands the range of proteins that can bind to the ScaA-based enzyme complex.
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