TY - JOUR
T1 - Ruminococcal cellulosome systems from rumen to human
AU - Ben David, Yonit
AU - Dassa, Bareket
AU - Borovok, Ilya
AU - Lamed, Raphael
AU - Koropatkin, Nicole M.
AU - Martens, Eric C.
AU - White, Bryan A.
AU - Bernalier-Donadille, Annick
AU - Duncan, Sylvia H.
AU - Flint, Harry J.
AU - Bayer, Edward A.
AU - Moraïs, Sarah
N1 - Publisher Copyright:
© 2015 Society for Applied Microbiology and John Wiley & Sons Ltd.
PY - 2015/9/1
Y1 - 2015/9/1
N2 - 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.
AB - 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.
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U2 - 10.1111/1462-2920.12868
DO - 10.1111/1462-2920.12868
M3 - Article
C2 - 25845888
AN - SCOPUS:84941024989
SN - 1462-2912
VL - 17
SP - 3407
EP - 3426
JO - Environmental Microbiology
JF - Environmental Microbiology
IS - 9
ER -