Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a  -glucosidase

Lin, Long-Liu; Rumbak, Elaine; Zappe, Harold; Thomson, Jennifer A.; Woods, David R.

doi:10.1099/00221287-136-8-1567

Cited by 52 publications

(25 citation statements)

References 40 publications

(20 reference statements)

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“…Consistenly with the B. jhri.soloc~.s and R. albus enzymes characteristics, it is remarkable that these anaerobic bacteria /3-glucosidases are grouped together in the phylogenetic analysis. These results agree with the literature which reports similarities between Butyrivibrio~brisolvm.s and Kluyveromyces fragilis, Clostridium Themocellutn and Cundidu pelliculosa sequences [6]. Of course the behaviour of B. jihri- Table 1 Summary of cloned B-.glucosidases sub-family B solvens and R. albus /3-glucosidases requieres attention.…”

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confidence: 89%

A sequence analysis of the β‐glucosidase sub‐family B

Rojas

Romeu

1996

FEBS Letters

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This computational study is a summary of structural properties of the fi-glucosidase subfamily B. Computations were carried out using GCG package programs. All sequences used in this analysis were taken from the protein data bank. The multialignment and the phylogenetic tree of the P-glucosidase subfamily B are shown. The conserved patterns: DGP, GRNFE, DPYL, KHF, SDW, GLD, VLLKN in the N-terminal region and FGYGLSY in the C-terminal part should be pointed out. Cterminal parts of the ButyrivibrioJibrisolvens and Ruminoccocus albus @-glucosidase sequences can be aligned to the N-terminal region of the other members of the subfamily. A crossed homology model in sub-family B P-glucosidases is described.

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Section: Fig 1 (Cord)supporting

confidence: 89%

A sequence analysis of the β‐glucosidase sub‐family B

Rojas

Romeu

1996

FEBS Letters

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“…A similar putative promoter sequence was reported in an endoglucanase gene from R. albus AR67 (26), but this promoter was shown to be functional in E. coli and not in R. albus AR67. Other studies of RNA transcribed in E. coli have also shown the occurrence of multiple transcription initiation sites for genes from the ruminal bacteria Prevotella ruminicola (14) and Butyrivibrio fibrisolvens (13).…”

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confidence: 88%

Albusin B, a Bacteriocin from the Ruminal Bacterium Ruminococcus albus 7 That Inhibits Growth of Ruminococcus flavefaciens

Chen

Stevenson

Weimer

2004

Appl Environ Microbiol

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An ϳ32-kDa protein (albusin B) that inhibited growth of Ruminococcus flavefaciens FD-1 was isolated from culture supernatants of Ruminococcus albus 7. Traditional cloning and gene-walking PCR techniques revealed an open reading frame (albB) encoding a protein with a predicted molecular mass of 32,168 Da. A BLAST search revealed two homologs of AlbB from the unfinished genome of R. albus 8 and moderate similarity to LlpA, a recently described 30-kDa bacteriocin from Pseudomonas sp. strain BW11M1.Ruminococcus albus and Ruminococcus flavefaciens are important cellulose-degrading bacteria in the rumen (6). R. albus has been reported to outnumber R. flavefaciens in defined laboratory cocultures (4,16,17,22) and in the rumens of sheep (25) and dairy cattle (28). Several reports suggested that predominance of R. albus may be due to its production of bacteriocin-like substances (4,16,17), but none of these agents had been purified. The objective of this study was to purify and characterize bacteriocin-like substances produced by R. albus.Culture supernatants of R. albus 7 grown in modified Dehority medium (27) with cellulose or cellobiose as a fermentable carbohydrate inhibited growth of R. flavefaciens FD-1 when assayed by a plate culture assay (4). Because most of the bacteriocins purified from gram-positive bacteria have low molecular masses (Ͻ10 kDa), we examined filtrates of R. albus 7 cultures for inhibitory activity toward R. flavefaciens. Cultures grown in 10 liters of modified Dehority medium with cellobiose were passed through a 0.2-m-pore-size hollow fiber cartridge, and the filtrate was passed through a 10-kDa-molecular-masscutoff cartridge. Substantial inhibitory activity was observed in the nominal 10-kDa filtrate, but surprisingly this filtrate contained a 32-kDa protein (referred to here as albusin B) that was ultimately shown to account for most of the activity. Although the retentate from the 10-kDa cartridge also contained an inhibitory protein of 32 kDa, the mixture of components in the retentate was far more complex than that in the filtrate. The simple protein profile of the filtrate facilitated purification of albusin B, which was accomplished by a process that also included ammonium sulfate precipitation (40 to 60% saturation range) and a BioGel P6 gel filtration column (Table 1). Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis revealed a single protein band (32 kDa) from the P6 column (Fig. 1). While the purification was facilitated by the 10-kDa-molecular-mass-cutoff ultrafiltration step, the complete protocol resulted in only a 4.7% activity yield and an estimated purification of 220-fold. Because some of the inhibitory activity in culture supernatants was due to a second inhibitor (albusin A, which will be described elsewhere), whose concentration declined during the course of the purification, the extent of purification of albusin B must be regarded as a lower bound.All seven R. flavefaciens strains tested (FD-1, B34b, 17, C94, B1c45, B146, and R13e2) were sensitive to albusi...

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“…Indirect selection was used by Okita et al (38) to clone the glg genes by cotransformation with the selectable asd (aspartate semidehydrogenase) gene which is adjacent to the glg gene cluster. Kiel et al (27) isolated the glgB gene from the cyanobacterium BUTYRIVIBRIO FIBRISOLVENS glgB GENE 6733 been described previously (32). B. fibrisolvens H17c was grown in M10 medium as described by Strydom et al (51).…”

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confidence: 99%

Characterization of the Butyrivibrio fibrisolvens glgB gene, which encodes a glycogen-branching enzyme with starch-clearing activity

et al. 1991

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(calculated Mr, 73,875) with 46 to 50% sequence homology with other branching enzymes. A limited region of 12 amino acids showed sequence similarity to amylases and glucanotransferases. The B. fibrisolvens branching enzyme was not able to hydrolyze starch but stimulated phosphorylase a-mediated incorporation of glucose into a-1,4-glucan polymer 13.4-fold. The branching enzyme was purified to homogeneity by a simple two-step procedure; N-terminal sequence and amino acid composition determinations confirmed the deduced translational start and amino acid sequence of the open reading frame. The enzymatic properties of the purified enzyme were investigated. The enzyme transferred chains of 5 to 10 (optimum, 7) glucose units, using amylose and amylopectin as substrates, to produce a highly branched polymer.

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Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a -glucosidase

Cited by 52 publications

References 40 publications

A sequence analysis of the β‐glucosidase sub‐family B

A sequence analysis of the β‐glucosidase sub‐family B

Albusin B, a Bacteriocin from the Ruminal Bacterium Ruminococcus albus 7 That Inhibits Growth of Ruminococcus flavefaciens

Characterization of the Butyrivibrio fibrisolvens glgB gene, which encodes a glycogen-branching enzyme with starch-clearing activity

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