Gene array analysis of Yersinia enterocolitica FlhD and FlhC: regulation of enzymes affecting synthesis and degradation of carbamoylphosphate.
This paper focuses on global gene regulation by FlhD/FlhC in enteric bacteria. Even though Yersinia enterocolitica FlhD/FlhC can complement an Escherichia coli flhDC mutant for motility, it is not known if the Y. enterocolitica FlhD/FlhC complex has an effect on metabolism similar to E. coli. To study metabolic gene regulation, a partial Yersinia enterocolitica 8081c microarray was constructed and the expression patterns of wild-type cells were compared to an flhDC mutant strain at 25 and 37 degrees C. The overlap between the E. coli and Y. enterocolitica FlhD/FlhC regulated genes was 25 %. Genes that were regulated at least fivefold by FlhD/FlhC in Y. enterocolitica are genes encoding urocanate hydratase (hutU), imidazolone propionase (hutI), carbamoylphosphate synthetase (carAB) and aspartate carbamoyltransferase (pyrBI). These enzymes are part of a pathway that is involved in the degradation of L-histidine to L-glutamate and eventually leads into purine/pyrimidine biosynthesis via carbamoylphosphate and carbamoylaspartate. A number of other genes were regulated at a lower rate. In two additional experiments, the expression of wild-type cells grown at 4 or 25 degrees C was compared to the same strain grown at 37 degrees C. The expression of the flagella master operon flhD was not affected by temperature, whereas the flagella-specific sigma factor fliA was highly expressed at 25 degrees C and reduced at 4 and 37 degrees C. Several other flagella genes, all of which are under the control of FliA, exhibited a similar temperature profile. These data are consistent with the hypothesis that temperature regulation of flagella genes might be mediated by the flagella-specific sigma factor FliA and not the flagella master regulator FlhD/FlhC.
Kapatral
Vinayak
V
Integrated Genomics, Inc., 2201 West Campbell Park Dr., Chicago, IL 60612, USA.
Campbell
John W
JW
Integrated Genomics, Inc., 2201 West Campbell Park Dr., Chicago, IL 60612, USA.
Minnich
Scott A
SA
Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, ID 83843, USA.
Thomson
Nicholas R
NR
The Wellcome Trust Sanger Institute, Genome Campus, Hinxton, Cambridge CB10 1RQ, UK.
Matsumura
Philip
P
Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7344, USA.
Prüß
Birgit M
BM
Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7344, USA.
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002221:Carbamyl Phosphate / Q000378:metabolism*; D003470:Culture Media; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D005407:Flagella / Q000502:physiology; D020869:Gene Expression Profiling; D015964:Gene Expression Regulation, Bacterial; D009154:Mutation; D020411:Oligonucleotide Array Sequence Analysis / Q000379:methods*; D016133:Polymerase Chain Reaction; D013696:Temperature; D015534:Trans-Activators / Q000235:genetics* / Q000378:metabolism; D015008:Yersinia enterocolitica / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000378:metabolism
D001426:Bacterial Proteins; D003470:Culture Media; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D015534:Trans-Activators; C090552:flhC protein, E coli; C090553:flhD protein, E coli; D002221:Carbamyl Phosphate