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. 1995 Feb;177(3):854–857. doi: 10.1128/jb.177.3.854-857.1995

Regulated expression of the histidase structural gene in Streptomyces griseus.

P C Wu 1, K V Srinivasan 1, K E Kendrick 1
PMCID: PMC176672  PMID: 7836328

Abstract

The histidase structural gene from Streptomyces griseus was expressed from a leaderless, monocistronic transcript. Multiple copies of the DNA located upstream of the hutH transcription initiation site led to a significant level of histidase activity when present in trans in the wild-type strain grown under noninducing conditions.

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Selected References

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  1. Atkinson M. R., Wray L. V., Jr, Fisher S. H. Activation of the Bacillus subtilis hut operon at the onset of stationary growth phase in nutrient sporulation medium results primarily from the relief of amino acid repression of histidine transport. J Bacteriol. 1993 Jul;175(14):4282–4289. doi: 10.1128/jb.175.14.4282-4289.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bascarán V., Hardisson C., Braña A. F. Isolation and characterization of nitrogen-deregulated mutants of Streptomyces clavuligerus. J Gen Microbiol. 1989 Sep;135(9):2475–2482. doi: 10.1099/00221287-135-9-2475. [DOI] [PubMed] [Google Scholar]
  3. Betlach M., Friedman J., Boyer H. W., Pfeifer F. Characterization of a halobacterial gene affecting bacterio-opsin gene expression. Nucleic Acids Res. 1984 Oct 25;12(20):7949–7959. doi: 10.1093/nar/12.20.7949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bewsey K. E., Johnson M. E., Huff J. P. Rapid isolation and purification of DNA from agarose gels: the phenol-freeze-fracture method. Biotechniques. 1991 Jun;10(6):724–725. [PubMed] [Google Scholar]
  5. Blanck A., Oesterhelt D. The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin. EMBO J. 1987 Jan;6(1):265–273. doi: 10.1002/j.1460-2075.1987.tb04749.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Brown K. L., Wood S., Buttner M. J. Isolation and characterization of the major vegetative RNA polymerase of Streptomyces coelicolor A3(2); renaturation of a sigma subunit using GroEL. Mol Microbiol. 1992 May;6(9):1133–1139. doi: 10.1111/j.1365-2958.1992.tb01551.x. [DOI] [PubMed] [Google Scholar]
  8. Buttner M. J. RNA polymerase heterogeneity in Streptomyces coelicolor A3(2). Mol Microbiol. 1989 Nov;3(11):1653–1659. doi: 10.1111/j.1365-2958.1989.tb00151.x. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Dunn R., McCoy J., Simsek M., Majumdar A., Chang S. H., Rajbhandary U. L., Khorana H. G. The bacteriorhodopsin gene. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6744–6748. doi: 10.1073/pnas.78.11.6744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. Janssen G. R., Bibb M. J. Derivatives of pUC18 that have BglII sites flanking a modified multiple cloning site and that retain the ability to identify recombinant clones by visual screening of Escherichia coli colonies. Gene. 1993 Feb 14;124(1):133–134. doi: 10.1016/0378-1119(93)90774-w. [DOI] [PubMed] [Google Scholar]
  14. Jones R. L., 3rd, Jaskula J. C., Janssen G. R. In vivo translational start site selection on leaderless mRNA transcribed from the Streptomyces fradiae aph gene. J Bacteriol. 1992 Jul;174(14):4753–4760. doi: 10.1128/jb.174.14.4753-4760.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kaminskas E., Kimhi Y., Magasanik B. Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. J Biol Chem. 1970 Jul 25;245(14):3536–3544. [PubMed] [Google Scholar]
  16. Katz E., Thompson C. J., Hopwood D. A. Cloning and expression of the tyrosinase gene from Streptomyces antibioticus in Streptomyces lividans. J Gen Microbiol. 1983 Sep;129(9):2703–2714. doi: 10.1099/00221287-129-9-2703. [DOI] [PubMed] [Google Scholar]
  17. Kendrick K. E., Wheelis M. L. Histidine dissimilation in Streptomyces coelicolor. J Gen Microbiol. 1982 Sep;128(9):2029–2040. doi: 10.1099/00221287-128-9-2029. [DOI] [PubMed] [Google Scholar]
  18. Klock G., Hillen W. Expression, purification and operator binding of the transposon Tn1721-encoded Tet repressor. J Mol Biol. 1986 Jun 20;189(4):633–641. doi: 10.1016/0022-2836(86)90493-6. [DOI] [PubMed] [Google Scholar]
  19. Kroening T. A., Kendrick K. E. Cascading regulation of histidase activity in Streptomyces griseus. J Bacteriol. 1989 Feb;171(2):1100–1105. doi: 10.1128/jb.171.2.1100-1105.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kroening T. A., Kendrick K. E. In vivo regulation of histidine ammonia-lyase activity from Streptomyces griseus. J Bacteriol. 1987 Feb;169(2):823–829. doi: 10.1128/jb.169.2.823-829.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lessie T. G., Neidhardt F. C. Formation and operation of the histidine-degrading pathway in Pseudomonas aeruginosa. J Bacteriol. 1967 Jun;93(6):1800–1810. doi: 10.1128/jb.93.6.1800-1810.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Macaluso A., Best E. A., Bender R. A. Role of the nac gene product in the nitrogen regulation of some NTR-regulated operons of Klebsiella aerogenes. J Bacteriol. 1990 Dec;172(12):7249–7255. doi: 10.1128/jb.172.12.7249-7255.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Oda M., Katagai T., Tomura D., Shoun H., Hoshino T., Furukawa K. Analysis of the transcriptional activity of the hut promoter in Bacillus subtilis and identification of a cis-acting regulatory region associated with catabolite repression downstream from the site of transcription. Mol Microbiol. 1992 Sep;6(18):2573–2582. doi: 10.1111/j.1365-2958.1992.tb01434.x. [DOI] [PubMed] [Google Scholar]
  25. 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]
  26. Osuna R., Boylan S. A., Bender R. A. In vitro transcription of the histidine utilization (hutUH) operon from Klebsiella aerogenes. J Bacteriol. 1991 Jan;173(1):116–123. doi: 10.1128/jb.173.1.116-123.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. 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]
  28. Ptashne M., Backman K., Humayun M. Z., Jeffrey A., Maurer R., Meyer B., Sauer R. T. Autoregulation and function of a repressor in bacteriophage lambda. Science. 1976 Oct 8;194(4261):156–161. doi: 10.1126/science.959843. [DOI] [PubMed] [Google Scholar]
  29. 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]
  30. Strohl W. R. Compilation and analysis of DNA sequences associated with apparent streptomycete promoters. Nucleic Acids Res. 1992 Mar 11;20(5):961–974. doi: 10.1093/nar/20.5.961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Ward J. M., Janssen G. R., Kieser T., Bibb M. J., Buttner M. J., Bibb M. J. Construction and characterisation of a series of multi-copy promoter-probe plasmid vectors for Streptomyces using the aminoglycoside phosphotransferase gene from Tn5 as indicator. Mol Gen Genet. 1986 Jun;203(3):468–478. doi: 10.1007/BF00422072. [DOI] [PubMed] [Google Scholar]
  32. Wray L. V., Jr, Pettengill F. K., Fisher S. H. Catabolite repression of the Bacillus subtilis hut operon requires a cis-acting site located downstream of the transcription initiation site. J Bacteriol. 1994 Apr;176(7):1894–1902. doi: 10.1128/jb.176.7.1894-1902.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Wu P. C., Kroening T. A., White P. J., Kendrick K. E. Purification of histidase from Streptomyces griseus and nucleotide sequence of the hutH structural gene. J Bacteriol. 1992 Mar;174(5):1647–1655. doi: 10.1128/jb.174.5.1647-1655.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]

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