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. 1988 Sep;170(9):4097–4102. doi: 10.1128/jb.170.9.4097-4102.1988

Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis.

T Nohno 1, Y Kasai 1, T Saito 1
PMCID: PMC211414  PMID: 3045084

Abstract

The nucleotide sequence of a HinPI-HpaII restriction nuclease fragment which complemented a delta chlE strain of Escherichia coli was determined. Two open reading frames were deduced to be the structural genes for ChlE and ChlN proteins, which have molecular weights of 44,067 and 26,719, respectively. Both proteins were required for complementing a chromosomal deletion of the chlE locus. The chlE and chlN genes were transcribed from a common promoter, chlEp, located upstream of chlE. Transcriptional and translational signal sequences were recognized in this region.

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Selected References

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

  1. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Biggin M. D., Gibson T. J., Hong G. F. Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination. Proc Natl Acad Sci U S A. 1983 Jul;80(13):3963–3965. doi: 10.1073/pnas.80.13.3963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bonnefoy-Orth V., Lepelletier M., Pascal M. C., Chippaux M. Nitrate reductase and cytochrome bnitrate reductase structural genes as parts of the nitrate reductase operon. Mol Gen Genet. 1981;181(4):535–540. doi: 10.1007/BF00428749. [DOI] [PubMed] [Google Scholar]
  4. Chippaux M., Bonnefoy-Orth V., Ratouchniak J., Pascal M. C. Operon fusions in the nitrate reductase operon and study of the control gene nir R in Escherichia coli. Mol Gen Genet. 1981;182(3):477–479. doi: 10.1007/BF00293938. [DOI] [PubMed] [Google Scholar]
  5. Edwards E. S., Rondeau S. S., DeMoss J. A. chlC (nar) operon of Escherichia coli includes structural genes for alpha and beta subunits of nitrate reductase. J Bacteriol. 1983 Mar;153(3):1513–1520. doi: 10.1128/jb.153.3.1513-1520.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Grosjean H., Fiers W. Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene. 1982 Jun;18(3):199–209. doi: 10.1016/0378-1119(82)90157-3. [DOI] [PubMed] [Google Scholar]
  7. Ingledew W. J., Poole R. K. The respiratory chains of Escherichia coli. Microbiol Rev. 1984 Sep;48(3):222–271. doi: 10.1128/mr.48.3.222-271.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Iuchi S., Lin E. C. The narL gene product activates the nitrate reductase operon and represses the fumarate reductase and trimethylamine N-oxide reductase operons in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3901–3905. doi: 10.1073/pnas.84.11.3901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Johann S., Hinton S. M. Cloning and nucleotide sequence of the chlD locus. J Bacteriol. 1987 May;169(5):1911–1916. doi: 10.1128/jb.169.5.1911-1916.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Johnson J. L., Hainline B. E., Rajagopalan K. V., Arison B. H. The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J Biol Chem. 1984 May 10;259(9):5414–5422. [PubMed] [Google Scholar]
  11. Johnson J. L., Hainline B. E., Rajagopalan K. V. Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component. J Biol Chem. 1980 Mar 10;255(5):1783–1786. [PubMed] [Google Scholar]
  12. Johnson M. E., Rajagopalan K. V. In vitro system for molybdopterin biosynthesis. J Bacteriol. 1987 Jan;169(1):110–116. doi: 10.1128/jb.169.1.110-116.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Johnson M. E., Rajagopalan K. V. Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis. J Bacteriol. 1987 Jan;169(1):117–125. doi: 10.1128/jb.169.1.117-125.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lambden P. R., Guest J. R. Mutants of Escherichia coli K12 unable to use fumarate as an anaerobic electron acceptor. J Gen Microbiol. 1976 Dec;97(2):145–160. doi: 10.1099/00221287-97-2-145. [DOI] [PubMed] [Google Scholar]
  16. MacGregor C. H. Synthesis of nitrate reductase components in chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1975 Mar;121(3):1117–1121. doi: 10.1128/jb.121.3.1117-1121.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Masters P. S., Hong J. S. Genetics of the glutamine transport system in Escherichia coli. J Bacteriol. 1981 Sep;147(3):805–819. doi: 10.1128/jb.147.3.805-819.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Merino E., Becerril B., Valle F., Bolivar F. Deletion of a repetitive extragenic palindromic (REP) sequence downstream from the structural gene of Escherichia coli glutamate dehydrogenase affects the stability of its mRNA. Gene. 1987;58(2-3):305–309. doi: 10.1016/0378-1119(87)90386-6. [DOI] [PubMed] [Google Scholar]
  19. Miller J. B., Amy N. K. Molybdenum cofactor in chlorate-resistant and nitrate reductase-deficient insertion mutants of Escherichia coli. J Bacteriol. 1983 Aug;155(2):793–801. doi: 10.1128/jb.155.2.793-801.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mizusawa S., Nishimura S., Seela F. Improvement of the dideoxy chain termination method of DNA sequencing by use of deoxy-7-deazaguanosine triphosphate in place of dGTP. Nucleic Acids Res. 1986 Feb 11;14(3):1319–1324. doi: 10.1093/nar/14.3.1319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Newbury S. F., Smith N. H., Robinson E. C., Hiles I. D., Higgins C. F. Stabilization of translationally active mRNA by prokaryotic REP sequences. Cell. 1987 Jan 30;48(2):297–310. doi: 10.1016/0092-8674(87)90433-8. [DOI] [PubMed] [Google Scholar]
  22. Nohno T., Saito T., Hong J. S. Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ). Mol Gen Genet. 1986 Nov;205(2):260–269. doi: 10.1007/BF00430437. [DOI] [PubMed] [Google Scholar]
  23. Nohno T., Saito T. Two transcriptional start sites found in the promoter region of Escherichia coli glutamine permease operon, glnHPQ. Nucleic Acids Res. 1987 Mar 25;15(6):2777–2777. doi: 10.1093/nar/15.6.2777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Pascal M. C., Burini J. F., Ratouchniak J., Chippaux M. Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes. Mol Gen Genet. 1982;188(1):103–106. doi: 10.1007/BF00333001. [DOI] [PubMed] [Google Scholar]
  25. Pascal M. C., Chippaux M. Involvement of a gene of the chl E locus in the regulation of the nitrate reductase operon. Mol Gen Genet. 1982;185(2):334–338. doi: 10.1007/BF00330808. [DOI] [PubMed] [Google Scholar]
  26. Rondeau S. S., Hsu P. Y., DeMoss J. A. Construction in vitro of a cloned nar operon from Escherichia coli. J Bacteriol. 1984 Jul;159(1):159–166. doi: 10.1128/jb.159.1.159-166.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. 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]
  28. Shaw D. J., Guest J. R. Amplification and product identification of the fnr gene of Escherichia coli. J Gen Microbiol. 1982 Oct;128(10):2221–2228. doi: 10.1099/00221287-128-10-2221. [DOI] [PubMed] [Google Scholar]
  29. Shine J., Dalgarno L. Determinant of cistron specificity in bacterial ribosomes. Nature. 1975 Mar 6;254(5495):34–38. doi: 10.1038/254034a0. [DOI] [PubMed] [Google Scholar]
  30. Sperl G. T., DeMoss J. A. chlD gene function in molybdate activation of nitrate reductase. J Bacteriol. 1975 Jun;122(3):1230–1238. doi: 10.1128/jb.122.3.1230-1238.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Stern M. J., Ames G. F., Smith N. H., Robinson E. C., Higgins C. F. Repetitive extragenic palindromic sequences: a major component of the bacterial genome. Cell. 1984 Jul;37(3):1015–1026. doi: 10.1016/0092-8674(84)90436-7. [DOI] [PubMed] [Google Scholar]
  32. Stewart V., MacGregor C. H. Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci. J Bacteriol. 1982 Aug;151(2):788–799. doi: 10.1128/jb.151.2.788-799.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Venables W. A. Genetic studies with nitrate reductase-less mutants of Escherichia coli. I. Fine structure analysis of the narA, narB and narE loci. Mol Gen Genet. 1972;114(3):223–231. doi: 10.1007/BF01788891. [DOI] [PubMed] [Google Scholar]
  34. Venables W. A., Guest J. R. Transduction of nitrate reductase loci of Escherichia coli by phages P-1 and lambda. Mol Gen Genet. 1968;103(2):127–140. doi: 10.1007/BF00427140. [DOI] [PubMed] [Google Scholar]

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