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High-frequency transfer of a naturally occurring chromosomal tetracycline resistance element in the ruminal anaerobe Butyrivibria fibrisolvens

Article Abstract:

Microbiological research has established the presence of a transmissible chromosomal element with tetracycline resistance in the obligately anaerobic rumen bacterial species Butyrivibrio fibrisolvens. Pulsed-field gel electrophoretic analysis demonstrates the transconjugant's altered chromosomal band profile. Evidence suggests that a distantly related Tc(super r) genetic determinant is transferred.

Author: Scott, Karen P., Flint, Harry J., Barbosa, Teresa M., Forbes, Kenneth J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
Tetracyclines, Rumen, Rumen microbiology, Transfer factor (Immunology), Transfer factor

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Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences

Article Abstract:

Results demonstrate that all three esterase domains share amino acid sequence identity between them, exhibit dockerin-like regions, and catalytic domains. Data further indicate that dockerin from two of the esterases differ significantly and perhaps represent distinct specificities to dockerin.

Author: Aurilia, Vincenzo, Martin, Jennifer C., McCrae, Sheila I., Scott, Karen P., Rincon, Marco T., Flint, Harry J.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
United Kingdom, United States, Statistical Data Included, Physiological aspects, Esterases, Enzymes, Microbial metabolism, Amino acids, Enzyme structure-activity relationships, Amino acid structure-activity relationships

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EndB, a multidomain family 44 cellulase from Ruminococcus flavefaciens 17, binds to cellulose via a novel celluloase-binding module and to another R. flavefaciens protein via a dockerin domain

Article Abstract:

The properties of the 808-amino acid cellulase produced by the endB gene in Ruminococcus flavefaciens 17 are described. The EndB protein may bind to celluloase via a cellulose-binding module or via its involvement in a cellulosome-like multienzyme complex.

Author: Kirby, James, McCrae, Sheila I., Scott, Karen P., Rincon, Marco T., Flint, Harry J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Microbiology, Microbial enzymes, Cellulose

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