Mapping, cloning, and DNA sequencing of pepB which encodes peptidase B of Escherichia coli K-12

Journal of Fermentation and Bioengineering

Volumn 82, Issue 4, 1996, Pages 392-397

  Suzuki, Hideyuki ^a   Kim, Eun Soo ^a,b   Yamamoto, Nagi ^a   Hashimoto, Wataru ^a   Yamamoto, Kenji ^a   Kumagai, Hidehiko ^a  

^a KYOTO UNIVERSITY   (Japan)

^b Byakka Co   (South Korea)

Author keywords

aminopeptidase; cloning; DNA sequence; Escherichia coli; metal binding site; metallopeptidase; peptidase

Indexed keywords

AMINOPEPTIDASE; METALLOPROTEINASE; PEPTIDASE;

ARTICLE; DNA SEQUENCE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE FREQUENCY; GENE MAPPING; GENE MUTATION; GENETIC TRANSDUCTION; MOLECULAR CLONING; SALMONELLA TYPHIMURIUM;

ESCHERICHIA; ESCHERICHIA COLI K12; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0029906730     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0922-338X(96)89157-4     Document Type: Article

References (35)

1. Miller, C. G. and Schwartz, G.: Peptidase-deficient mutants of Escherichia coll. J. Bacteriol., 135, 603-611 (1978).
2. Miller, C. G.: Genetics and physiological roles of Salmonella typhimurium peptidases. Microbiology-1985, 346-349 (1985).
3. Miller, C. G.: Protein degradation and proteolytic modification, p. 680-691. In Neidhardt, F. C., Ingraham, J. L., Low, K. B., Magasanik, B., Schaechter, M., and Umbarger, H. E. (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C. (1987).
4. Stirling, C. J., Colloms, S. D., Collins, J. F., Szatmari, G., and Sherratt, D. J.: xerB, an Escherichia coli gene required for plasmid Co1E1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J., 8, 1623-1627 (1989).
5. Klein, J., Henrich, B., and Plapp, R.: Cloning and expression of the pepD gene of Escherichia coli. J. Gen. Microbiol., 132, 2337-2343 (1986).
6. Henrich, B., Monnerjahn, U., and Plapp, R.: Peptidase D gene (pepD) of Escherichia coli K-12: nucleotide sequence, transcript mapping, and comparison with other peptidase genes. J. Bacteriol., 172, 4641-4651 (1990).
7. McCaman, M. T. and Villarejo, M. R.: Structural and catalytic properties of peptidase N from Escherichia coli. Arch. Biochem. Biophys., 213, 384-394 (1982).
8. McCaman, M. T. and Gabe, J. D.: The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli. Gene, 48, 145-153 (1986).
9. Foglino, M., Gharbi, S., and Lazdunski, A.: Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli. Gene, 49, 303-309 (1986).
10. Miller, J. H.: Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York (1972).
11. Suzuki, H., Kumagai, H., and Tochikura, T.: Isolation, genetic mapping, and characterization of Escherichia coli K-12 mutants lacking γ-glutamyltranspeptidase. J. Bacteriol., 169, 3926-3931 (1987).
12. Singer, M., Baker, T. A., Schnitzler, G., Deischel, S. M., Goel, M., Dove, W., Jaacks, K. J., Grossman, A., Erickson, J. W., and Gross. C. A.: A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol. Rev., 53, 1-24 (1989).
13. Maniatis, T., Fritsch, E. F., and Sambrook, J.: Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York (1982).
14. Sanger, F., Nicklen, S., and Coulson, A. R.: DNA sequencing with chain-terminating inhibitor. Proc. Natl. Acad. Sci. USA, 74, 5463-5467 (1977).
15. Umbarger, H. E.: The biosynthesis of isoleucine and valine and its regulation, p. 245-266. In Herrmann, K. and Somerville, R. L. (eds.), Amino acids: biosynthesis and genetic regulation. Addison-Wesley, Reading, MA (1983).
16. Henrich, B. and Plapp, R.: Locations of the genes from pepD through proA on the physical map of the Escherichia coli chromosome. J. Bacteriol., 173, 7407-7408 (1991).
17. Latil, M., Murgier, M., Lazdunski, A., and Lazdunski, C.: Isolation and genetic mapping of Escherichia coli aminopeptidase mutants. Mol. Gen. Genet., 148, 43-47 (1976).
18. McCaman, M. T., McPartland, A., and Villarejo, M. R.: Genetics and regulation of peptidase N in Escherichia coli K-12. J. Bacteriol., 152, 848-854 (1982).
19. Green, L. and Miller, C. G.: Genetic mapping of the Salmonella typhimurium pepB locus. J. Bacteriol., 143, 1524-1526 (1980).
20. Sanderson, K. E. and Roth, J. R.: Linkage map of Salmonella typhimurium, edition VII. Microbiol. Rev., 52, 485-532 (1988).
21. Clarke, L. and Carbon, J.: Selection of specific clones from colony banks by suppression or complementation tests. Methods Enzymol., 68, 396-408 (1979).
22. Nishimura, A., Akiyama, K., Kohara, Y., and Horiuchi, K.: Correlation of a subset of the pLC plasmids to the physical map of Escherichia coli K-12. Microbiol. Rev., 56, 137-151 (1992).
23. Davis, D. J.: Disc electrophoresis-II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci., 121, 404-427 (1964).
24. Miller, CG. and Mackinnon, K.: Peptidase mutants of Salmonella typhimurium. J. Bacteriol., 120, 355-363 (1974).
25. Kohara, Y., Akiyama, K., and Isono, K.: The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell, 50, 495-508 (1987).
26. Chang, A. C. and Cohen, S. N.: Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol., 134, 1141-1156 (1978).
27. Maeda, T., Tachi, K., Kojima, K., and Okayama, T.: Two-dimensional electrophoresis of plasma proteins without denaturing agents. J. Biochem., 85, 649-659 (1979).
28. Hirano, H.: Microsequence analysis of proteins electroblotted from polyacrylamide gels. Protein, Nucl. Acid Enzyme, 33, 2388-2396 (1988).
29. Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J.: Basic local alignment search tool. J. Mol. Biol., 215, 403-410 (1990).
30. Kawula, T. H. and Lelivelt, M. J.: Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli. J. Bacteriol., 176, 610-619 (1994).
31. Shine, J. and Dalgarno, L.: The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding site. Proc. Natl. Acad. Sci. USA, 71, 1342-1346 (1974).
32. Kim, H. and Lipscomb, W. N.: Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography. Proc. Natl. Acad. Sci. USA, 90, 5006-5010 (1993).
33. McCulloch, R., Burke, M. E., and Sherratt, D. J.: Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination. Mol. Microbiol., 12, 241-251 (1994).
34. Rawlings, N. D. and Barrett, A. J.: Evolutionary families of metallopeptidases. Methods Enzymol., 248, 183-228 (1995).
35. van Loon-Klassen, L., Cuypers, H. T., and Bloemendal, H.: Limited tryptic digestion of bovine eye lens leucine aminopeptidase. FEBS Lett., 107, 366-370 (1979).