Determination of a 17484 bp nucleotide sequence around the 39° region of the Bacillus subtilis chromosome and similarity analysis of the products of putative ORFs

References

1. Adachi T., Mizuuchi M., Robinson E.A., Appella E., O’Dea M.H., Gellert M., Mizuuchi K. 1987; DNA sequence of the E. coli gyrB gene: application of a new sequencing strategy.. Nucleic Acids Res 15:771–784
   [Google Scholar]
2. Anagnostopoulos C., Piggot P.J., Hoch J.A. 1993; The genetic map of Bacillus subtilis. . In Bacillus subtilis and Other GramPositive Bacteria: Biochemistry, Physiology and Molecular Genetics pp. 425–461 Sonenshein A.L., Hoch J.A., Losick R. Edited by Washington, DC: American Society for Microbiology;
   [Google Scholar]
3. Asoh S., Matsuzawa H., Ishino F., Strominger J.C., Matsuhashi M., Ohta H. 1986; Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillinbinding protein 2 of Escherichia coli K12.. Eur J Biochem 160:231–238
   [Google Scholar]
4. Chaudhry G.R., Halpern Y.S., Saunders C., Vasantha N., Schmidt B.J., Freese E. 1984; Mapping of the glucose dehydrogenase gene in Bacillus subtilis.. J Bacteriol 160:607–611
   [Google Scholar]
5. Davis T., Yamada M., Elgort M., Saier M.H. Jr 1988; Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli.. Mol Microbiol 2:405–412
   [Google Scholar]
6. Ding M., Yelton D.B. 1993; Cloning and analysis of the leuB gene of Eeptospira interrogans serovar pomona.. J Gen Microbiol 139:1093–1103
   [Google Scholar]
7. Fischer R., Hengtenberg W. 1992; Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: sequence and expression in Escherichia coli and structural comparison with the enzyme n^mannito1 of Escherichia coli.. Eur J Biochem 204:963–969
   [Google Scholar]
8. Galinier A., Nègre D., Cortay J.C., Marcandier S., Maloy S.R., Cozzone A.J. 1990; Sequence analysis of the iclR gene encoding the repressor of the acetate operon in Salmonella typhimurium.. Nucleic Acids Res 18:3656
   [Google Scholar]
9. Genbauffe F.F., Cooper T.T. 1991; The urea amidolyase (DUR1, 2) gene of Saccharomyces cerevisiae.. DNA Seq 2:19–32
   [Google Scholar]
10. Godon J.-J., Chopin M.-C., Ehrlich S.D. 1992; Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp.lactis.. J Bacteriol 174:6580–6589
    [Google Scholar]
11. Hawkins C.F., Borges A., Perham R.N. 1990; Cloning and sequence analysis of the genes encoding the a and p subunit of El component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermopbilus.. Eur J Biochem 191:337–346
    [Google Scholar]
12. Honeyman A.L., Curtiss R. III 1992; Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol- phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system.. Inject Immun 60:3369–3375
    [Google Scholar]
13. Imai R., Sekiguchi T., Nosoh Y., Tsuda K. 1987; The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from Bacillus subtilis.. Nucleic Acids Res 15:4988
    [Google Scholar]
14. Itaya M., Tanaka T. 1991; Complete physical map of the Bacillus subtilis 168 chromosome constructed by a gene-directed mutagenesis method.. J Mol Biol 220:631–648
    [Google Scholar]
15. Lee C.A., Saier M.H. Jr 1983; Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene.. J Biol Chem 258:10761–10767
    [Google Scholar]
16. March P.E., Inouye M. 1985; Characterization of the lep operon of Escherichia coli: identification of the promoter and the gene upstream of the signal peptidase I gene.. J Biol Chem 260:7206–7213
    [Google Scholar]
17. Ochman H., Gerber A.S., Hartl D.L. 1988; Genetic application of an inverse polymerase chain reaction.. Genetics 120:621–623
    [Google Scholar]
18. Ogawa K., Akagawa E., Nakamura K., Yamane K. 1995; Determination of a 21548 bp nucleotide sequence around the 24° region of the Bacillus subtilis chromosome.. Microbiology 141:269–275
    [Google Scholar]
19. Richardson I.B., Katz M.E., Hynes M.J. 1992; Molecular characterization of the lam locus and sequence involved in regulation by the amdR protein of Aspergillus nidulans.. Mol Cell Biol 12:337–346
    [Google Scholar]
20. Ryffel C., Tesch W., Birch-Machin I., Reynolds P.E., Barbleris-Maino L., Kayser F.H., Berger-Bächi B. 1990; Sequence comparison of mecA gene isolated from methicillin-resistant Staphylococcus aureus and Staphylococcus epidermidis.. Gene 94:137–138
    [Google Scholar]
21. Sambrook J., Fritsch E.F., Maniatis T. 1989 Molecular Cloning: A Laboratory Manual, 2nd edn.. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
22. Sekiguchi T., Ortega-Cesena J., Nosoh Y., Ohashi S., Tsuda K., Kanaya S. 1986; DNA and amino acid sequences of 3-iso- propylmalate dehydrogenase of Bacillus coagulans. Comparison with the enzymes of Saccharomyces cerevisiae and Thermus thermophilus.. Biochim Biophys Acta 867:36–44
    [Google Scholar]
23. Smith C.P., Chater K.F. 1988; Structure and regulation of controlling sequences for the Streptomyces coelicolor glycerol operon.. J Mol Biol 204:569–580
    [Google Scholar]
24. Sorokin A., Zumstein E., Azevedo V., Ehrlich S.D., Serror P. 1993; The organization of the Bacillus subtilis 168 chromosome region between the spo VA and serA genetic loci, based on sequence data.. Mol Microbiol 10:385–395
    [Google Scholar]
25. Sunnarborg A., Klumpp D., Chung T., LaPort D.C. 1990; Regulation of the glyoxylate bypass operon: cloning and charac-terization of iclR.. J Bacteriol 172:2642–2649
    [Google Scholar]
26. van Dijl J.M., de Jong A., Vehmaanperä J., Venema G., Bron S. 1992; Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases.. EMBO J 11:2819–2828
    [Google Scholar]
27. van Dijl J.M., de Jong A., Venema G., Bron S. 1995; Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis: structural and functional similarities with LexA- like proteases.. J Biol Chem 270:3611–3618
    [Google Scholar]