ArticleJournal of bacteriology1995
OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domains to components of the cell envelope.
Article in Journal of bacteriology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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63 citing papers in PubMed, 166 citations in OpenAlex.
- Rapid adaptation for fibre degradation by changes in plasmid stoichiometry within Lactobacillus plantarum at the synthetic community level.Microbial biotechnology · 2020Article
- Constructing a yeast to express the largest cellulosome complex on the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Biomimetic strategy for constructingBiotechnology for biofuels · 2018Article
- Cellulosomes: bacterial nanomachines for dismantling plant polysaccharides.Nature reviews. Microbiology · 2017Review
- Unique organization and unprecedented diversity of theBiotechnology for biofuels · 2017Article
- Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species.The Journal of biological chemistry · 2016Article
- Cel5I, a SLH-Containing Glycoside Hydrolase: Characterization and Investigation on Its Role in Ruminiclostridium cellulolyticum.PloS one · 2016Article
- Article
- Driving biomass breakdown through engineered cellulosomes.Bioengineered · 2015Review
- S-layers: principles and applications.FEMS microbiology reviews · 2014Article
- Cellulosomics of the cellulolytic thermophile Clostridium clariflavum.Biotechnology for biofuels · 2014Article
- Article
- Are the surface layer homology domains essential for cell surface display and glycosylation of the S-layer protein from Paenibacillus alvei CCM 2051T?Journal of bacteriology · 2013Article
- Role of the CipA scaffoldin protein in cellulose solubilization, as determined by targeted gene deletion and complementation in Clostridium thermocellum.Journal of bacteriology · 2013Article
- Article
- Effects of synthetic cohesin-containing scaffold protein architecture on binding dockerin-enzyme fusions on the surface of Lactococcus lactis.Microbial cell factories · 2012Article
- Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome.The Journal of biological chemistry · 2012Article
- Genome-wide analysis of acetivibrio cellulolyticus provides a blueprint of an elaborate cellulosome system.BMC genomics · 2012Article
- Nanopods: a new bacterial structure and mechanism for deployment of outer membrane vesicles.PloS one · 2011Article
- Engineering the cell surface display of cohesins for assembly of cellulosome-inspired enzyme complexes on Lactococcus lactis.Microbial cell factories · 2010Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several proteins of Clostridium thermocellum possess a C-terminal triplicated sequence related to bacterial cell surface proteins. This sequence was named the SLH domain (for S-layer homology), and it was proposed that it might serve to anchor proteins to the cell surface (A. Lupas, H. Engelhardt, J. Peters, U. Santarius, S. Volker, and W. Baumeister, J. Bacteriol. 176:1224-1233, 1994). This hypothesis was investigated by using the SLH-containing protein ORF1p from C. thermocellum as a model. Subcellular fractionation, immunoblotting, and electron microscopy of immunocytochemically labeled cells indicated that ORF1p was located on the surface of C. thermocellum. To detect C. thermocellum components interacting with the SLH domains of ORF1p, a probe was constructed by grafting these domains on the C terminus of the MalE protein of Escherichia coli. The SLH domains conferred on the chimeric protein (MalE-ORF1p-C) the ability to bind noncovalently to the peptidoglycan of C. thermocellum. In addition, 125I-labeled MalE-ORF1p-C was shown to bind to SLH-bearing proteins transferred onto nitrocellulose, and to a 26- to 28-kDa component of the cell envelope. These results agree with the hypothesis that SLH domains contribute to the binding of exocellular proteins to the cell surface of bacteria. The gene carrying ORF1 and its product, ORF1p, are renamed olpB and OlpB (for outer layer protein B), respectively.
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