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J Biol Chem, Vol. 273, Issue 48, 31788-31794, November 27, 1998
From the Department of Bacteriology, University of Wisconsin,
Madison, Wisconsin 53706-1567
The cobB gene of
Salmonella typhimurium LT2 has been isolated and
genetically and biochemically characterized. cobB was
located by genetic means to the 27-centisome region of the chromosome. Genetic crosses established the gene order to be cobB pepT
phoQ, and the direction of cobB transcription was
shown to be clockwise. The nucleotide sequence of cobB (711 base pairs) predicted a protein of 237 amino acids length with a
molecular mass of 26.3 kDa, a mass consistent with the experimentally
determined one of ~28 kDa. The cobB gene was defined
genetically by deletions (), insertions (), and point mutations
(). The precise location of a Tn10d(Tc) element within
cobB was established by sequencing. DNA sequence analysis
of the region flanking cobB located it 81 base pairs 3' of
the potABCD operon, with the potABCD operon and cobB being divergently transcribed. cobB was
overexpressed to ~30% of the total soluble protein using a T7
overexpression system. In vitro activity assays showed that
cell-free extracts enriched for CobB catalyzed the synthesis of the
cobalamin biosynthetic intermediate
N1-(5-phospho-
CobB, a New Member of the SIR2 Family of Eucaryotic Regulatory
Proteins, Is Required to Compensate for the Lack of Nicotinate
Mononucleotide:5,6-Dimethylbenzimidazole Phosphoribosyltransferase
Activity in cobT Mutants during Cobalamin Biosynthesis in
Salmonella typhimurium LT2
-D-ribosyl)-5,6-dimethylbenzimidazole
(also known as -ribazole-5'-phosphate) from nicotinate
mononucleotide and 5,6-dimethylbenzimidazole, the reaction known to be
catalyzed by the CobT phosphoribosyltransferase enzyme (EC 2.4.2.21)
(Trzebiatowski, J. R. and Escalante-Semerena, J. C. (1997)
J. Biol. Chem. 272, 17662-17667). Computer analysis
of the primary amino acid sequence of the CobB protein identified the
sequences GAGISAESGIRTFR and YTQNID which are diagnostic of members of the SIR2 family
of eucaryotic transcriptional regulators. Possible roles of CobB as a
regulator are discussed within the context of the catabolism of
propionate, a pathway known to require cobB function
(Tsang, A. W. and Escalante-Semerena, J. C. (1996)
J. Bacteriol. 178, 7016-7019).
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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