Ribose utilization by the human commensal Bifidobacterium breve UCC2003

Typeset version

 

TY  - JOUR
  - Pokusaeva, K,Neves, AR,Zomer, A,O'Connell-Motherway, M,MacSharry, J,Curley, P,Fitzgerald, GF,van Sinderen, D
  - 2010
  - January
  - Microbial Biotechnology
  - Ribose utilization by the human commensal Bifidobacterium breve UCC2003
  - Validated
  - ()
  - ESCHERICHIA-COLI K-12 BACILLUS-SUBTILIS GASTROINTESTINAL-TRACT GENE-EXPRESSION FUNCTIONAL ANALYSES IN-VIVO PREBIOTICS IDENTIFICATION METABOLISM PROTEIN
  - 3
  - 311
  - 323
  - Growth of Bifidobacterium breve UCC2003 on ribose leads to the transcriptional induction of the rbsACBDK gene cluster. Generation and phenotypic analysis of an rbsA insertion mutant established that the rbs gene cluster is essential for ribose utilization, and that its transcription is likely regulated by a LacI-type regulator encoded by rbsR, located immediately upstream of rbsA. Gel mobility shift assays using purified RbsR(His) indicate that the promoter upstream of rbsABCDK is negatively controlled by RbsRHis binding to an 18 bp inverted repeat and that RbsRHis binding activity is modulated by D-ribose. The rbsK gene of the rbs operon of B. breve UCC2003 was shown to specify a ribokinase (EC 2.7.1.15), which specifically directs its phosphorylating activity towards D-ribose, converting this pentose sugar to ribose-5-phosphate.
  - DOI 10.1111/j.1751-7915.2009.00152.x
DA  - 2010/01
ER  - 
@article{V90194252,
   = {Pokusaeva,  K and Neves,  AR and Zomer,  A and O'Connell-Motherway,  M and MacSharry,  J and Curley,  P and Fitzgerald,  GF and van Sinderen,  D },
   = {2010},
   = {January},
   = {Microbial Biotechnology},
   = {Ribose utilization by the human commensal Bifidobacterium breve UCC2003},
   = {Validated},
   = {()},
   = {ESCHERICHIA-COLI K-12 BACILLUS-SUBTILIS GASTROINTESTINAL-TRACT GENE-EXPRESSION FUNCTIONAL ANALYSES IN-VIVO PREBIOTICS IDENTIFICATION METABOLISM PROTEIN},
   = {3},
  pages = {311--323},
   = {{Growth of Bifidobacterium breve UCC2003 on ribose leads to the transcriptional induction of the rbsACBDK gene cluster. Generation and phenotypic analysis of an rbsA insertion mutant established that the rbs gene cluster is essential for ribose utilization, and that its transcription is likely regulated by a LacI-type regulator encoded by rbsR, located immediately upstream of rbsA. Gel mobility shift assays using purified RbsR(His) indicate that the promoter upstream of rbsABCDK is negatively controlled by RbsRHis binding to an 18 bp inverted repeat and that RbsRHis binding activity is modulated by D-ribose. The rbsK gene of the rbs operon of B. breve UCC2003 was shown to specify a ribokinase (EC 2.7.1.15), which specifically directs its phosphorylating activity towards D-ribose, converting this pentose sugar to ribose-5-phosphate.}},
   = {DOI 10.1111/j.1751-7915.2009.00152.x},
  source = {IRIS}
}
AUTHORSPokusaeva, K,Neves, AR,Zomer, A,O'Connell-Motherway, M,MacSharry, J,Curley, P,Fitzgerald, GF,van Sinderen, D
YEAR2010
MONTHJanuary
JOURNAL_CODEMicrobial Biotechnology
TITLERibose utilization by the human commensal Bifidobacterium breve UCC2003
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORDESCHERICHIA-COLI K-12 BACILLUS-SUBTILIS GASTROINTESTINAL-TRACT GENE-EXPRESSION FUNCTIONAL ANALYSES IN-VIVO PREBIOTICS IDENTIFICATION METABOLISM PROTEIN
VOLUME3
ISSUE
START_PAGE311
END_PAGE323
ABSTRACTGrowth of Bifidobacterium breve UCC2003 on ribose leads to the transcriptional induction of the rbsACBDK gene cluster. Generation and phenotypic analysis of an rbsA insertion mutant established that the rbs gene cluster is essential for ribose utilization, and that its transcription is likely regulated by a LacI-type regulator encoded by rbsR, located immediately upstream of rbsA. Gel mobility shift assays using purified RbsR(His) indicate that the promoter upstream of rbsABCDK is negatively controlled by RbsRHis binding to an 18 bp inverted repeat and that RbsRHis binding activity is modulated by D-ribose. The rbsK gene of the rbs operon of B. breve UCC2003 was shown to specify a ribokinase (EC 2.7.1.15), which specifically directs its phosphorylating activity towards D-ribose, converting this pentose sugar to ribose-5-phosphate.
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EDITION
URL
DOI_LINKDOI 10.1111/j.1751-7915.2009.00152.x
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