A second gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae

Biochemical and Biophysical Research Communications

Volumn 228, Issue 2, 1996, Pages 452-458

  Nozaki, Takako ^b   Nishimura, Ken ^b   Michael, Anthony J ^a,b   Maruyama, Takaharu ^b   Kakinuma, Yoshimi ^b   Igarashi, Kazuei ^b  

^a INSTITUTE OF FOOD RESEARCH   (United Kingdom)

^b CHIBA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MAGNESIUM; PROTEIN SERINE THREONINE KINASE; SPERMINE;

AMINE TRANSPORT; AMINO ACID SEQUENCE; ARTICLE; DEPHOSPHORYLATION; FUNGUS MUTANT; GENE ISOLATION; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PHOSPHORYLATION; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; X CHROMOSOME;

FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0343373759     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.1681     Document Type: Article

References (20)

1. 1. Kakinuma, Y., Maruyama, T., Nozaki, T., Wada, Y., Ohsumi, Y., and Igarashi, K. (1995) Biochem. Biophys. Res. Commun. 216, 985-992.
2. 2. Igarashi, K., and Kashiwagi, K. (1996) Amino Acids 10, 83-97.
3. 3. Kano, K., and Oka, T. (1976) J. Biol. Chem. 251, 2795-2880.
4. 4. Kakinuma, Y., Hoshino, K., and Igarashi, K. (1988) Eur. J. Biochem. 176, 409-414.
5. 5. Davis, R. H., and Ristow, J. L. (1988) Arch. Biochem. Biophys. 267, 479-489.
6. 6. Maruyama, T., Masuda, N., Kakinuma, Y., and Igarashi, K. (1994) Biochim. Biophys. Acta 1194, 289-295.
7. 7. He, Y., Kashiwagi, K., Fukuchi, J., Terao, K., Shirahata, A., and Igarashi, K. (1993) Eur. J. Biochem. 217, 89-96.
8. 8. Suzuki, T., He, Y., Kashiwagi, K., Murakami, Y., Hayashi, S.-I., and Igarashi, K. (1994) Proc. Natl. Acad. Sci. USA 91, 8930-8934.
9. 9. He, Y., Suzuki, T., Kashiwagi, K., and Igarashi, K. (1994) Biochem. Biophys. Res. Commun. 203, 608-614.
10. 10. Mitchell, J. L. A., Judd, G. G., Bareyal-Leyser, A., and Ling, S. Y. (1994) Biochem. J. 299, 19-22.
11. 11. Sherman, F. (1991) Methods Enzymol. 194, 3-21.
12. 12. Yoshihisa, T., and Anraku, Y. (1989) Biochem. Biophys. Res. Commun. 163, 908-915.
13. 13. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. USA 74, 5463-5467.
14. 14. Ausubel, F. M., Brent, R., Kingstone, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K. (1987) Current Protocols in Molecular Biology. Green, New York.
15. 15. Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983) J. Bacteriol. 153, 163-168.
16. 16. Kakinuma, Y., Masuda, N., and Igarashi, K. (1992) Biochim. Biophys. Acta 1107, 126-130.
17. 17. Galibert, F. et al. (1996) EMBO J. 15, 2031-2049.
18. 18. Kyte, J., and Doolittle, R. F. (1982) J. Mol. Biol. 157, 105-132.
19. 19. Hanks, S. K., and Quinn, A. M. (1991) Methods Enzymol. 200, 38-62.
20. 20. Dujon, B. et al. (1994) Nature 369, 371-378.