Ribose utilization by the human commensal Bifidobacterium breve UCC2003

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 regula...

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Main Authors: Pokusaeva, Karina, Neves, Ana Rute, Zomer, Aldert, O'Connell‐Motherway, Mary, MacSharry, John, Curley, Peter, Fitzgerald, Gerald F., Van Sinderen, Douwe
Format: Online
Language:English
Published: Blackwell Publishing Ltd 2010
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815373/
id pubmed-3815373
recordtype oai_dc
spelling pubmed-38153732014-02-12 Ribose utilization by the human commensal Bifidobacterium breve UCC2003 Pokusaeva, Karina Neves, Ana Rute Zomer, Aldert O'Connell‐Motherway, Mary MacSharry, John Curley, Peter Fitzgerald, Gerald F. Van Sinderen, Douwe Research Articles 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 RbsRHis 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. Blackwell Publishing Ltd 2010-05 2010-04-20 /pmc/articles/PMC3815373/ /pubmed/21255330 http://dx.doi.org/10.1111/j.1751-7915.2009.00152.x Text en Copyright© 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Pokusaeva, Karina
Neves, Ana Rute
Zomer, Aldert
O'Connell‐Motherway, Mary
MacSharry, John
Curley, Peter
Fitzgerald, Gerald F.
Van Sinderen, Douwe
spellingShingle Pokusaeva, Karina
Neves, Ana Rute
Zomer, Aldert
O'Connell‐Motherway, Mary
MacSharry, John
Curley, Peter
Fitzgerald, Gerald F.
Van Sinderen, Douwe
Ribose utilization by the human commensal Bifidobacterium breve UCC2003
author_facet Pokusaeva, Karina
Neves, Ana Rute
Zomer, Aldert
O'Connell‐Motherway, Mary
MacSharry, John
Curley, Peter
Fitzgerald, Gerald F.
Van Sinderen, Douwe
author_sort Pokusaeva, Karina
title Ribose utilization by the human commensal Bifidobacterium breve UCC2003
title_short Ribose utilization by the human commensal Bifidobacterium breve UCC2003
title_full Ribose utilization by the human commensal Bifidobacterium breve UCC2003
title_fullStr Ribose utilization by the human commensal Bifidobacterium breve UCC2003
title_full_unstemmed Ribose utilization by the human commensal Bifidobacterium breve UCC2003
title_sort ribose utilization by the human commensal bifidobacterium breve ucc2003
description 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 RbsRHis 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.
publisher Blackwell Publishing Ltd
publishDate 2010
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815373/
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