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. 1994 Sep;176(17):5474–5482. doi: 10.1128/jb.176.17.5474-5482.1994

The control region of the pdu/cob regulon in Salmonella typhimurium.

P Chen 1, D I Andersson 1, J R Roth 1
PMCID: PMC196736  PMID: 8071226

Abstract

The pdu operon encodes proteins for the catabolism of 1,2-propanediol; the nearby cob operon encodes enzymes for the biosynthesis of adenosyl-cobalamin (vitamin B12), a cofactor required for the use of propanediol. These operons are transcribed divergently from distinct promoters separated by several kilobases. The regulation of the two operons is tightly integrated in that both require the positive activator protein PocR and both are subject to global control by the Crp and ArcA proteins. We have determined the DNA nucleotide sequences of the promoter-proximal portion of the pdu operon and the region between the pdu and cob operons. Four open reading frames have been identified, pduB, pduA, pduF, and pocR. The pduA and pduB genes are the first two genes of the pdu operon (transcribed clockwise). The pduA gene encodes a hydrophobic protein with 56% amino acid identity to a 10.9-kDa protein which serves as a component of the carboxysomes of several photosynthetic bacteria. The pduF gene encodes a hydrophobic protein with a strong similarity to the GlpF protein of Escherichia coli, which facilitates the diffusion of glycerol. The N-terminal end of the PduF protein includes a motif for a membrane lipoprotein-lipid attachment site as well as a motif characteristic of the MIP (major intrinsic protein) family of transmembrane channel proteins. We presume that the PduF protein facilitates the diffusion of propanediol. The pocR gene encodes the positive regulatory protein of the cob and pdu operons and shares the helix-turn-helix DNA binding motif of the AraC family of regulatory proteins. The mutations cobR4 and cobR58 cause constitutive, pocR-independent expression of the cob operon under both aerobic and anaerobic conditions. Evidence that each mutation is a deletion creating a new promoter near the normal promoter site of the cob operon is presented.

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Selected References

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  1. Ailion M., Bobik T. A., Roth J. R. Two global regulatory systems (Crp and Arc) control the cobalamin/propanediol regulon of Salmonella typhimurium. J Bacteriol. 1993 Nov;175(22):7200–7208. doi: 10.1128/jb.175.22.7200-7208.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Andersson D. I. Involvement of the Arc system in redox regulation of the Cob operon in Salmonella typhimurium. Mol Microbiol. 1992 Jun;6(11):1491–1494. doi: 10.1111/j.1365-2958.1992.tb00869.x. [DOI] [PubMed] [Google Scholar]
  3. Andersson D. I., Roth J. R. Mutations affecting regulation of cobinamide biosynthesis in Salmonella typhimurium. J Bacteriol. 1989 Dec;171(12):6726–6733. doi: 10.1128/jb.171.12.6726-6733.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Andersson D. I., Roth J. R. Redox regulation of the genes for cobinamide biosynthesis in Salmonella typhimurium. J Bacteriol. 1989 Dec;171(12):6734–6739. doi: 10.1128/jb.171.12.6734-6739.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Baker M. E., Saier M. H., Jr A common ancestor for bovine lens fiber major intrinsic protein, soybean nodulin-26 protein, and E. coli glycerol facilitator. Cell. 1990 Jan 26;60(2):185–186. doi: 10.1016/0092-8674(90)90731-s. [DOI] [PubMed] [Google Scholar]
  6. Bobik T. A., Ailion M., Roth J. R. A single regulatory gene integrates control of vitamin B12 synthesis and propanediol degradation. J Bacteriol. 1992 Apr;174(7):2253–2266. doi: 10.1128/jb.174.7.2253-2266.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Brendel V., Trifonov E. N. A computer algorithm for testing potential prokaryotic terminators. Nucleic Acids Res. 1984 May 25;12(10):4411–4427. doi: 10.1093/nar/12.10.4411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cheng S. W., Lynch E. C., Leason K. R., Court D. L., Shapiro B. A., Friedman D. I. Functional importance of sequence in the stem-loop of a transcription terminator. Science. 1991 Nov 22;254(5035):1205–1207. doi: 10.1126/science.1835546. [DOI] [PubMed] [Google Scholar]
  9. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Escalante-Semerena J. C., Johnson M. G., Roth J. R. The CobII and CobIII regions of the cobalamin (vitamin B12) biosynthetic operon of Salmonella typhimurium. J Bacteriol. 1992 Jan;174(1):24–29. doi: 10.1128/jb.174.1.24-29.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Escalante-Semerena J. C., Roth J. R. Regulation of cobalamin biosynthetic operons in Salmonella typhimurium. J Bacteriol. 1987 May;169(5):2251–2258. doi: 10.1128/jb.169.5.2251-2258.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Farabaugh P. J., Schmeissner U., Hofer M., Miller J. H. Genetic studies of the lac repressor. VII. On the molecular nature of spontaneous hotspots in the lacI gene of Escherichia coli. J Mol Biol. 1978 Dec 25;126(4):847–857. doi: 10.1016/0022-2836(78)90023-2. [DOI] [PubMed] [Google Scholar]
  13. Fernández-Briera A., Garrido-Pertierra A. A degradation pathway of propionate in Salmonella typhimurium LT-2. Biochimie. 1988 Jun;70(6):757–768. doi: 10.1016/0300-9084(88)90105-8. [DOI] [PubMed] [Google Scholar]
  14. Frey B., McCloskey J., Kersten W., Kersten H. New function of vitamin B12: cobamide-dependent reduction of epoxyqueuosine to queuosine in tRNAs of Escherichia coli and Salmonella typhimurium. J Bacteriol. 1988 May;170(5):2078–2082. doi: 10.1128/jb.170.5.2078-2082.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Jeter R. M. Cobalamin-dependent 1,2-propanediol utilization by Salmonella typhimurium. J Gen Microbiol. 1990 May;136(5):887–896. doi: 10.1099/00221287-136-5-887. [DOI] [PubMed] [Google Scholar]
  16. Jeter R. M., Olivera B. M., Roth J. R. Salmonella typhimurium synthesizes cobalamin (vitamin B12) de novo under anaerobic growth conditions. J Bacteriol. 1984 Jul;159(1):206–213. doi: 10.1128/jb.159.1.206-213.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Jeter R. M., Roth J. R. Cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J Bacteriol. 1987 Jul;169(7):3189–3198. doi: 10.1128/jb.169.7.3189-3198.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  19. Muramatsu S., Mizuno T. Nucleotide sequence of the region encompassing the glpKF operon and its upstream region containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 1989 Jun 12;17(11):4378–4378. [PMC free article] [PubMed] [Google Scholar]
  20. Muto A., Osawa S. The guanine and cytosine content of genomic DNA and bacterial evolution. Proc Natl Acad Sci U S A. 1987 Jan;84(1):166–169. doi: 10.1073/pnas.84.1.166. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Obradors N., Badía J., Baldomà L., Aguilar J. Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium. J Bacteriol. 1988 May;170(5):2159–2162. doi: 10.1128/jb.170.5.2159-2162.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Price G. D., Howitt S. M., Harrison K., Badger M. R. Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp. strain PCC7942 involved in carboxysome assembly and function. J Bacteriol. 1993 May;175(10):2871–2879. doi: 10.1128/jb.175.10.2871-2879.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Richter-Dahlfors A. A., Andersson D. I. Cobalamin (vitamin B12) repression of the Cob operon in Salmonella typhimurium requires sequences within the leader and the first translated open reading frame. Mol Microbiol. 1992 Mar;6(6):743–749. doi: 10.1111/j.1365-2958.1992.tb01524.x. [DOI] [PubMed] [Google Scholar]
  25. Rondon M. R., Escalante-Semerena J. C. The poc locus is required for 1,2-propanediol-dependent transcription of the cobalamin biosynthetic (cob) and propanediol utilization (pdu) genes of Salmonella typhimurium. J Bacteriol. 1992 Apr;174(7):2267–2272. doi: 10.1128/jb.174.7.2267-2272.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Roof D. M., Roth J. R. Ethanolamine utilization in Salmonella typhimurium. J Bacteriol. 1988 Sep;170(9):3855–3863. doi: 10.1128/jb.170.9.3855-3863.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Roof D. M., Roth J. R. Functions required for vitamin B12-dependent ethanolamine utilization in Salmonella typhimurium. J Bacteriol. 1989 Jun;171(6):3316–3323. doi: 10.1128/jb.171.6.3316-3323.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Roth J. R., Lawrence J. G., Rubenfield M., Kieffer-Higgins S., Church G. M. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J Bacteriol. 1993 Jun;175(11):3303–3316. doi: 10.1128/jb.175.11.3303-3316.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Smith D. A., Childs J. D. Methionine genes and enzymes of Salmonella typhimurium. Heredity (Edinb) 1966 May;21(2):265–286. doi: 10.1038/hdy.1966.22. [DOI] [PubMed] [Google Scholar]
  31. Sweet G., Gandor C., Voegele R., Wittekindt N., Beuerle J., Truniger V., Lin E. C., Boos W. Glycerol facilitator of Escherichia coli: cloning of glpF and identification of the glpF product. J Bacteriol. 1990 Jan;172(1):424–430. doi: 10.1128/jb.172.1.424-430.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Toraya T., Honda S., Fukui S. Fermentation of 1,2-propanediol with 1,2-ethanediol by some genera of Enterobacteriaceae, involving coenzyme B12-dependent diol dehydratase. J Bacteriol. 1979 Jul;139(1):39–47. doi: 10.1128/jb.139.1.39-47.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  34. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  35. Yamamoto Y. T., Cheng C. L., Conkling M. A. Root-specific genes from tobacco and Arabidopsis homologous to an evolutionarily conserved gene family of membrane channel proteins. Nucleic Acids Res. 1990 Dec 25;18(24):7449–7449. doi: 10.1093/nar/18.24.7449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Youderian P., Sugiono P., Brewer K. L., Higgins N. P., Elliott T. Packaging specific segments of the Salmonella chromosome with locked-in Mud-P22 prophages. Genetics. 1988 Apr;118(4):581–592. doi: 10.1093/genetics/118.4.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Zhu Y., Lin E. C. L-1,2-propanediol exits more rapidly than L-lactaldehyde from Escherichia coli. J Bacteriol. 1989 Feb;171(2):862–867. doi: 10.1128/jb.171.2.862-867.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]

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