title: Ruminococcal cellulosome systems from rumen to human.
abstract: A cellulolytic fiber-degrading bacterium, Ruminococcus champanellensis, was isolated from human faecal samples, and its genome was recently sequenced. Bioinformatic analysis of the R. champanellensis genome revealed numerous cohesin and dockerin modules, the basic elements of the cellulosome, and manual sequencing of partially sequenced genomic segments revealed two large tandem scaffoldin-coding genes that form part of a gene cluster. Representative R. champanellensis dockerins were tested against putative cohesins, and the results revealed three different cohesin-dockerin binding profiles which implied two major types of cellulosome architectures: (i) an intricate cell-bound system and (ii) a simplistic cell-free system composed of a single cohesin-containing scaffoldin. The cell-bound system can adopt various enzymatic architectures, ranging from a single enzyme to a large enzymatic complex comprising up to 11 enzymes. The variety of cellulosomal components together with adaptor proteins may infer a very tight regulation of its components. The cellulosome system of the human gut bacterium R. champanellensis closely resembles that of the bovine rumen bacterium Ruminococcus flavefaciens. The two species contain orthologous gene clusters comprising fundamental components of cellulosome architecture. Since R. champanellensis is the only human colonic bacterium known to degrade crystalline cellulose, it may thus represent a keystone species in the human gut.
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
authors.forename: Yonit
authors.initials: Y
authors.lastname: Ben David
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
authors.forename: Bareket
authors.initials: B
authors.lastname: Dassa
authors.affiliation: Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel.
authors.forename: Ilya
authors.initials: I
authors.lastname: Borovok
authors.affiliation: Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel.
authors.forename: Raphael
authors.initials: R
authors.lastname: Lamed
authors.affiliation: Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.
authors.forename: Nicole M
authors.initials: NM
authors.lastname: Koropatkin
authors.affiliation: Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.
authors.forename: Eric C
authors.initials: EC
authors.lastname: Martens
authors.affiliation: Department of Animal Sciences and Institute for Genomic Biology, University of Illinois, Urbana, IL, USA.
authors.forename: Bryan A
authors.initials: BA
authors.lastname: White
authors.affiliation: Unite de Microbiologie UR454, INRA, CR de Clermont-Ferrand/Theix, Saint-Genes Champanelle, France.
authors.forename: Annick
authors.initials: A
authors.lastname: Bernalier-Donadille
authors.affiliation: Microbiology Group, Rowett Institute of Nutrition and Health, University of Aberdeen, Aberdeen, UK.
authors.forename: Sylvia H
authors.initials: SH
authors.lastname: Duncan
authors.affiliation: Microbiology Group, Rowett Institute of Nutrition and Health, University of Aberdeen, Aberdeen, UK.
authors.forename: Harry J
authors.initials: HJ
authors.lastname: Flint
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
authors.forename: Edward A
authors.initials: EA
authors.lastname: Bayer
authors.affiliation: Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
authors.forename: Sarah
authors.initials: S
authors.lastname: Moraïs
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000145:classification / Q000235:genetics*; D001483:Base Sequence; D002417:Cattle; D018797:Cell Cycle Proteins / Q000145:classification / Q000235:genetics*; D002482:Cellulose / Q000378:metabolism*; D044603:Cellulosomes / Q000235:genetics*; D002868:Chromosomal Proteins, Non-Histone / Q000145:classification / Q000235:genetics*; D004269:DNA, Bacterial / Q000235:genetics; D005243:Feces / Q000382:microbiology; D006801:Humans; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics* / Q000378:metabolism; D005810:Multigene Family / Q000235:genetics; D010802:Phylogeny; D012417:Rumen / Q000382:microbiology*; D045857:Ruminococcus / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D000097722:Cohesins
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D002482:Cellulose; D002868:Chromosomal Proteins, Non-Histone; D004269:DNA, Bacterial; D009097:Multienzyme Complexes; D000097722:Cohesins