rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2010-9-15
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pubmed:abstractText |
The genomes of Listeria spp. encode all but one of 25 enzymes required for the biosynthesis of adenosylcobalamin (AdoCbl; coenzyme B(12) ). Notably, all Listeria genomes lack CobT, the nicotinamide mononucleotide:5,6-dimethylbenzimidazole (DMB) phosphoribosyltransferase (EC 2.4.2.21) enzyme that synthesizes the unique ?-linked nucleotide N(1) -(5-phospho-?-D-ribosyl)-DMB (?-ribazole-5'-P, ?-RP), a precursor of AdoCbl. We have uncovered a new pathway for the synthesis of ?-RP in Listeria innocua that circumvents the lack of CobT. The cblT and cblS genes (locus tags lin1153 and lin1110) of L. innocua encode an ?-ribazole (?-R) transporter and an ?-R kinase respectively. Results from in vivo experiments indicate that L. innocua depends on CblT and CblS activities to salvage exogenous ?-R, allowing conversion of the incomplete corrinoid cobinamide (Cbi) into AdoCbl. Expression of the L. innocua cblT and cblS genes restored AdoCbl synthesis from Cbi and ?-R in a Salmonella enterica cobT strain. LinCblT transported ?-R across the cell membrane, but not ?-RP or DMB. UV-visible spectroscopy and mass spectrometry data identified ?-RP as the product of the ATP-dependent ?-R kinase activity of LinCblS. Bioinformatics analyses suggest that ?-R salvaging occurs in important Gram-positive human pathogens.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20633228-10508786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20633228-10518530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20633228-10873547,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20633228-9254694
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Benzimidazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Cobamides,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/N(1)-(5-phosphoribosyl)-5,6-dimethyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Pentosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleosides,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-ribazole,
http://linkedlifedata.com/resource/pubmed/chemical/cobinamide,
http://linkedlifedata.com/resource/pubmed/chemical/nicotinate-nucleotide-dimethylbenzim...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1365-2958
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pubmed:author |
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pubmed:copyrightInfo |
© 2010 Blackwell Publishing Ltd.
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pubmed:issnType |
Electronic
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pubmed:volume |
77
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1429-38
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pubmed:dateRevised |
2011-9-13
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pubmed:meshHeading |
pubmed-meshheading:20633228-Bacterial Proteins,
pubmed-meshheading:20633228-Benzimidazoles,
pubmed-meshheading:20633228-Cloning, Molecular,
pubmed-meshheading:20633228-Cobamides,
pubmed-meshheading:20633228-Computational Biology,
pubmed-meshheading:20633228-DNA, Bacterial,
pubmed-meshheading:20633228-Listeria,
pubmed-meshheading:20633228-Multienzyme Complexes,
pubmed-meshheading:20633228-Nucleotidyltransferases,
pubmed-meshheading:20633228-Pentosyltransferases,
pubmed-meshheading:20633228-Phosphorylation,
pubmed-meshheading:20633228-Plasmids,
pubmed-meshheading:20633228-Protein Kinases,
pubmed-meshheading:20633228-Ribonucleosides,
pubmed-meshheading:20633228-Ribonucleotides,
pubmed-meshheading:20633228-Salmonella enterica
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pubmed:year |
2010
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pubmed:articleTitle |
A new pathway for the synthesis of ?-ribazole-phosphate in Listeria innocua.
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pubmed:affiliation |
Department of Bacteriology, University of Wisconsin, 6478 Microbial Sciences Building, 1550 Linden Drive, Madison, WI 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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