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. 1997 Jun;63(6):2454–2459. doi: 10.1128/aem.63.6.2454-2459.1997

Cloning and sequence analysis of putative histidine protein kinases isolated from Lactococcus lactis MG1363.

M O'Connell-Motherway 1, G F Fitzgerald 1, D van Sinderen 1
PMCID: PMC168540  PMID: 9172368

Abstract

Eight recombinant plasmids harboring chromosomal fragments of Lactococcus lactis MG1363 were shown to phenotypically suppress a histidine protein kinase (HPK) deficiency in either of two different E. coli strains. Sequence analysis of the plasmid inserts revealed five different complete or partial open reading frames (ORFs) specifying proteins with high similarity to HPKs. One of the plasmids also harbored an additional ORF, unrelated to HPKs, with suppressing activity.

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Selected References

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  1. Aiba H., Nagaya M., Mizuno T. Sensor and regulator proteins from the cyanobacterium Synechococcus species PCC7942 that belong to the bacterial signal-transduction protein families: implication in the adaptive response to phosphate limitation. Mol Microbiol. 1993 Apr;8(1):81–91. doi: 10.1111/j.1365-2958.1993.tb01205.x. [DOI] [PubMed] [Google Scholar]
  2. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  3. BERTANI G. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol. 1951 Sep;62(3):293–300. doi: 10.1128/jb.62.3.293-300.1951. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Diep D. B., Håvarstein L. S., Nes I. F. Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J Bacteriol. 1996 Aug;178(15):4472–4483. doi: 10.1128/jb.178.15.4472-4483.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Diep D. B., Håvarstein L. S., Nissen-Meyer J., Nes I. F. The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system. Appl Environ Microbiol. 1994 Jan;60(1):160–166. doi: 10.1128/aem.60.1.160-166.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Effects of seawater cations and temperature on manganese dioxide-reductase activity in a marine bacillus. Appl Microbiol. 1975 Feb;29(2):307–307. doi: 10.1128/am.29.2.307-307.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hughes D. A. Signal transduction. Histidine kinases hog the limelight. Nature. 1994 May 19;369(6477):187–188. doi: 10.1038/369187a0. [DOI] [PubMed] [Google Scholar]
  9. Ishige K., Nagasawa S., Tokishita S., Mizuno T. A novel device of bacterial signal transducers. EMBO J. 1994 Nov 1;13(21):5195–5202. doi: 10.1002/j.1460-2075.1994.tb06850.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kuipers O. P., Beerthuyzen M. M., de Ruyter P. G., Luesink E. J., de Vos W. M. Autoregulation of nisin biosynthesis in Lactococcus lactis by signal transduction. J Biol Chem. 1995 Nov 10;270(45):27299–27304. doi: 10.1074/jbc.270.45.27299. [DOI] [PubMed] [Google Scholar]
  11. Lee P. J., Stock A. M. Characterization of the genes and proteins of a two-component system from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol. 1996 Oct;178(19):5579–5585. doi: 10.1128/jb.178.19.5579-5585.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Leenhouts K. J., Kok J., Venema G. Replacement recombination in Lactococcus lactis. J Bacteriol. 1991 Aug;173(15):4794–4798. doi: 10.1128/jb.173.15.4794-4798.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Maeda T., Wurgler-Murphy S. M., Saito H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature. 1994 May 19;369(6477):242–245. doi: 10.1038/369242a0. [DOI] [PubMed] [Google Scholar]
  14. Nagasawa S., Ishige K., Mizuno T. Novel members of the two-component signal transduction genes in Escherichia coli. J Biochem. 1993 Sep;114(3):350–357. doi: 10.1093/oxfordjournals.jbchem.a124180. [DOI] [PubMed] [Google Scholar]
  15. Nagasawa S., Tokishita S., Aiba H., Mizuno T. A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli. Mol Microbiol. 1992 Mar;6(6):799–807. doi: 10.1111/j.1365-2958.1992.tb01530.x. [DOI] [PubMed] [Google Scholar]
  16. Osbourn A. E., Clarke B. R., Stevens B. J., Daniels M. J. Use of oligonucleotide probes to identify members of two-component regulatory systems in Xanthomonas campestris pathovar campestris. Mol Gen Genet. 1990 Jun;222(1):145–151. doi: 10.1007/BF00283036. [DOI] [PubMed] [Google Scholar]
  17. Parkinson J. S., Kofoid E. C. Communication modules in bacterial signaling proteins. Annu Rev Genet. 1992;26:71–112. doi: 10.1146/annurev.ge.26.120192.000443. [DOI] [PubMed] [Google Scholar]
  18. Parkinson J. S. Signal transduction schemes of bacteria. Cell. 1993 Jun 4;73(5):857–871. doi: 10.1016/0092-8674(93)90267-t. [DOI] [PubMed] [Google Scholar]
  19. Rabin R. S., Stewart V. Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12. J Bacteriol. 1993 Jun;175(11):3259–3268. doi: 10.1128/jb.175.11.3259-3268.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Rabin R. S., Stewart V. Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8419–8423. doi: 10.1073/pnas.89.18.8419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Stewart V., Parales J., Jr, Merkel S. M. Structure of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12. J Bacteriol. 1989 Apr;171(4):2229–2234. doi: 10.1128/jb.171.4.2229-2234.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Stock J. B., Ninfa A. J., Stock A. M. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol Rev. 1989 Dec;53(4):450–490. doi: 10.1128/mr.53.4.450-490.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Utsumi R., Katayama S., Taniguchi M., Horie T., Ikeda M., Igaki S., Nakagawa H., Miwa A., Tanabe H., Noda M. Newly identified genes involved in the signal transduction of Escherichia coli K-12. Gene. 1994 Mar 11;140(1):73–77. doi: 10.1016/0378-1119(94)90733-1. [DOI] [PubMed] [Google Scholar]
  24. Wanner B. L. Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria? J Bacteriol. 1992 Apr;174(7):2053–2058. doi: 10.1128/jb.174.7.2053-2058.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]
  26. van der Meer J. R., Polman J., Beerthuyzen M. M., Siezen R. J., Kuipers O. P., De Vos W. M. Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis. J Bacteriol. 1993 May;175(9):2578–2588. doi: 10.1128/jb.175.9.2578-2588.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]

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