ArticleJournal of bacteriology2004
A novel Acetivibrio cellulolyticus anchoring scaffoldin that bears divergent cohesins.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 45 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
- Engineered Stochastic Adhesion Between Microbes as a Protection Mechanism Against Environmental Stress.Cellular and molecular bioengineering · 2018Article
- Structure-function analyses generate novel specificities to assemble the components of multienzyme bacterial cellulosome complexes.The Journal of biological chemistry · 2018Article
- Dramatic performance of Clostridium thermocellum explained by its wide range of cellulase modalities.Science advances · 2016Article
- Cell-surface Attachment of Bacterial Multienzyme Complexes Involves Highly Dynamic Protein-Protein Anchors.The Journal of biological chemistry · 2015Article
- Article
- Overexpression, purification, crystallization and preliminary X-ray characterization of the fourth scaffoldin A cohesin from Acetivibrio cellulolyticus in complex with a dockerin from a family 5 glycoside hydrolase.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Purification, crystallization and preliminary X-ray characterization of the third ScaB cohesin in complex with an ScaA X-dockerin from Acetivibrio cellulolyticus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Article
- Cellulosomics of the cellulolytic thermophile Clostridium clariflavum.Biotechnology for biofuels · 2014Article
- Proteinaceous determinants of surface colonization in bacteria: bacterial adhesion and biofilm formation from a protein secretion perspective.Frontiers in microbiology · 2013Review
- Purification, crystallization and preliminary X-ray characterization of the Acetivibrio cellulolyticus type I cohesin ScaC in complex with the ScaB dockerin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Genome-wide analysis of acetivibrio cellulolyticus provides a blueprint of an elaborate cellulosome system.BMC genomics · 2012Article
- Complete Genome Sequence of Clostridium clariflavum DSM 19732.Standards in genomic sciences · 2012Article
- Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Exploration of new geometries in cellulosome-like chimeras.Applied and environmental microbiology · 2007Article
- Conservation and divergence in cellulosome architecture between two strains of Ruminococcus flavefaciens.Journal of bacteriology · 2006Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sequencing of a cellulosome-integrating gene cluster in Acetivibrio cellulolyticus was completed. The cluster contains four tandem scaffoldin genes (scaA, scaB, scaC, and scaD) bounded upstream and downstream, respectively, by a presumed cellobiose phosphorylase and a nucleotide methylase. The sequences and properties of scaA, scaB, and scaC were reported previously, and those of scaD are reported here. The scaD gene encodes an 852-residue polypeptide that includes a signal peptide, three cohesins, and a C-terminal S-layer homology (SLH) module. The calculated molecular weight of the mature ScaD is 88,960; a 67-residue linker segment separates cohesins 1 and 2, and two approximately 30-residue linkers separate cohesin 2 from 3 and cohesin 3 from the SLH module. The presence of an SLH module in ScaD indicates its role as an anchoring protein. The first two ScaD cohesins can be classified as type II, similar to the four cohesins of ScaB. Surprisingly, the third ScaD cohesin belongs to the type I cohesins, like the seven ScaA cohesins. ScaD is the first scaffoldin to be described that contains divergent types of cohesins as integral parts of the polypeptide chain. The recognition properties among selected recombinant cohesins and dockerins from the different scaffoldins of the gene cluster were investigated by affinity blotting. The results indicated that the divergent types of ScaD cohesins also differ in their preference of dockerins. ScaD thus plays a dual role, both as a primary scaffoldin, capable of direct incorporation of a single dockerin-borne enzyme, and as a secondary scaffoldin that anchors the major primary scaffoldin, ScaA and its complement of enzymes to the cell surface.
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