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. 1990 Sep;172(9):5470–5476. doi: 10.1128/jb.172.9.5470-5476.1990

Nucleotide sequence of the gene encoding the repressor for the histidine utilization genes of Pseudomonas putida.

S L Allison 1, A T Phillips 1
PMCID: PMC213214  PMID: 2203753

Abstract

The hutC gene of Pseudomonas putida encodes a repressor which, in combination with the inducer urocanate, regulates expression of the five structural genes necessary for conversion of histidine to glutamate, ammonia, and formate. The nucleotide sequence of the hutC region was determined and found to contain two open reading frames which overlapped by one nucleotide. The first open reading frame (ORF1) appeared to encode a 27,648-dalton protein of 248 amino acids whose sequence strongly resembled that of the hut repressor of Klebsiella aerogenes (A. Schwacha and R. A. Bender, J. Bacteriol. 172:5477-5481, 1990) and contained a helix-turn-helix motif that could be involved in operator binding. The gene was preceded by a sequence which was nearly identical to that of the operator site located upstream of hutU which controls transcription of the hutUHIG genes. The operator near hutC would presumably allow the hut repressor to regulate its own synthesis as well as the expression of the divergent hutF gene. A second open reading frame (ORF2) would encode a 21,155-dalton protein, but because this region could be deleted with only a slight effect on repressor activity, it is not likely to be involved in repressor function or structure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beck C. F., Warren R. A. Divergent promoters, a common form of gene organization. Microbiol Rev. 1988 Sep;52(3):318–326. doi: 10.1128/mr.52.3.318-326.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bolivar F., Rodriguez R. L., Greene P. J., Betlach M. C., Heyneker H. L., Boyer H. W., Crosa J. H., Falkow S. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 1977;2(2):95–113. [PubMed] [Google Scholar]
  3. Boylan S. A., Bender R. A. Genetic and physical maps of Klebsiella aerogenes genes for histidine utilization (hut). Mol Gen Genet. 1984;193(1):99–103. doi: 10.1007/BF00327421. [DOI] [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Consevage M. W., Porter R. D., Phillips A. T. Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida. J Bacteriol. 1985 Apr;162(1):138–146. doi: 10.1128/jb.162.1.138-146.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Goldberg R. B., Magasanik B. Gene order of the histidine utilization (hut) operons in Klebsiella aerogenes. J Bacteriol. 1975 Jun;122(3):1025–1031. doi: 10.1128/jb.122.3.1025-1031.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hu L., Allison S. L., Phillips A. T. Identification of multiple repressor recognition sites in the hut system of Pseudomonas putida. J Bacteriol. 1989 Aug;171(8):4189–4195. doi: 10.1128/jb.171.8.4189-4195.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hu L., Mulfinger L. M., Phillips A. T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J Bacteriol. 1987 Oct;169(10):4696–4702. doi: 10.1128/jb.169.10.4696-4702.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hu L., Phillips A. T. Organization and multiple regulation of histidine utilization genes in Pseudomonas putida. J Bacteriol. 1988 Sep;170(9):4272–4279. doi: 10.1128/jb.170.9.4272-4279.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Johnson A. D., Pabo C. O., Sauer R. T. Bacteriophage lambda repressor and cro protein: interactions with operator DNA. Methods Enzymol. 1980;65(1):839–856. doi: 10.1016/s0076-6879(80)65078-2. [DOI] [PubMed] [Google Scholar]
  12. Kimhi Y., Magasanik B. Genetic basis of histidine degradation in Bacillus subtilis. J Biol Chem. 1970 Jul 25;245(14):3545–3548. [PubMed] [Google Scholar]
  13. Leidigh B. J., Wheelis M. L. Genetic control of the histidine dissimilatory pathway in Pseudomonas putida. Mol Gen Genet. 1973 Feb 2;120(3):201–210. doi: 10.1007/BF00267152. [DOI] [PubMed] [Google Scholar]
  14. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  15. Nieuwkoop A. J., Boylan S. A., Bender R. A. Regulation of hutUH operon expression by the catabolite gene activator protein-cyclic AMP complex in Klebsiella aerogenes. J Bacteriol. 1984 Sep;159(3):934–939. doi: 10.1128/jb.159.3.934-939.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Oda M., Sugishita A., Furukawa K. Cloning and nucleotide sequences of histidase and regulatory genes in the Bacillus subtilis hut operon and positive regulation of the operon. J Bacteriol. 1988 Jul;170(7):3199–3205. doi: 10.1128/jb.170.7.3199-3205.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pabo C. O., Sauer R. T. Protein-DNA recognition. Annu Rev Biochem. 1984;53:293–321. doi: 10.1146/annurev.bi.53.070184.001453. [DOI] [PubMed] [Google Scholar]
  18. Phillips A. T., Mulfinger L. M. Cyclic adenosine 3',5'-monophosphate levels in Pseudomonas putida and Pseudomonas aeruginosa during induction and carbon catabolite repression of histidase synthesis. J Bacteriol. 1981 Mar;145(3):1286–1292. doi: 10.1128/jb.145.3.1286-1292.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Potts J. R., Clarke P. H. The effect of nitrogen limitation on catabolite repression of amidase, histidase and urocanase in Pseudomonas aeruginosa. J Gen Microbiol. 1976 Apr;93(2):377–387. doi: 10.1099/00221287-93-2-377. [DOI] [PubMed] [Google Scholar]
  20. Prival M. J., Magasanik B. Resistance to catabolite repression of histidase and proline oxidase during nitrogen-limited growth of Klebsiella aerogenes. J Biol Chem. 1971 Oct 25;246(20):6288–6296. [PubMed] [Google Scholar]
  21. Rosenberg M., Court D. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet. 1979;13:319–353. doi: 10.1146/annurev.ge.13.120179.001535. [DOI] [PubMed] [Google Scholar]
  22. Rosenberg M., Ho Y. S., Shatzman A. The use of pKc30 and its derivatives for controlled expression of genes. Methods Enzymol. 1983;101:123–138. doi: 10.1016/0076-6879(83)01009-5. [DOI] [PubMed] [Google Scholar]
  23. Schwacha A., Bender R. A. Nucleotide sequence of the gene encoding the repressor for the histidine utilization genes of Klebsiella aerogenes. J Bacteriol. 1990 Sep;172(9):5477–5481. doi: 10.1128/jb.172.9.5477-5481.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Smith G. R., Magasanik B. The two operons of the histidine utilization system in Salmonella typhimurium. J Biol Chem. 1971 May 25;246(10):3330–3341. [PubMed] [Google Scholar]
  25. Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
  26. West S. E., Iglewski B. H. Codon usage in Pseudomonas aeruginosa. Nucleic Acids Res. 1988 Oct 11;16(19):9323–9335. doi: 10.1093/nar/16.19.9323. [DOI] [PMC free article] [PubMed] [Google Scholar]

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