Identification of a 22-kDa protein required for the degradation of selenomonas ruminantium Lysine decarboxylase by ATP-dependent protease

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 6, 2002, Pages 1431-1434

  Yamaguchi, Yoshihiro ^a   Takatsuka, Yumiko ^a   Kamio, Yoshiyuki ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

Antizyme; ATP dependent protease; Degradation of lysine decarboxylase (LDC); Regulator protein; Selenomonas ruminantium

Indexed keywords

BACTERIA (MICROORGANISMS); MAMMALIA; NEGIBACTERIA; OVIS ARIES; PROKARYOTA; SELENOMONAS; SELENOMONAS RUMINANTIUM;

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; BACTERIAL PROTEIN; CARBOXYLYASE; HEAT SHOCK PROTEIN; LYSINE DECARBOXYLASE; SERINE PROTEINASE;

ARTICLE; CHEMISTRY; CYTOLOGY; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN PROCESSING; SELENOMONAS; TIME;

ATP-DEPENDENT PROTEASES; BACTERIAL PROTEINS; CARBOXY-LYASES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HEAT-SHOCK PROTEINS; MOLECULAR WEIGHT; PROTEIN PROCESSING, POST-TRANSLATIONAL; SELENOMONAS; SERINE ENDOPEPTIDASES; TIME FACTORS;

EID: 0036616603     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1431     Document Type: Article

References (10)

1. Tabor, C. W. and Tabor, H., Polyamines in microorganisms. Microbiol. Rev., 49, 81-99 (1985).
2. dela Vega, A. L. and Delcour, A. H., Cadaverine induces closing of E. coli porins. EMBO J., 14, 6058-6065 (1995).
3. Kamio, Y., Itoh, Y., and Terawaki, Y., Chemical structure of peptidoglycan in Selenomonas ruminan-tium: cadaverine links covalently to the D-glutamic acid residue of peptidoglycan. J. Bacteriol., 146, 49-53 (1981).
4. Kamio, Y., Poso, H., Terawaki, Y., and Paulin, L., Cadaverine covalently linked to a peptidoglycan is an essential constituent of the peptidoglycan necessary for the normal growth in Selenomonas ruminantium. J. Biol. Chem., 261, 6585-6589 (1986).
5. Kamio, Y. and Nakamura, K., Putrescine and cadaverine are constituents of peptidoglycan in Veillonella alcalescens and Veillonella parvula. J. Bacteriol., 169, 2881-2884 (1987).
6. Hirao, T., Sato, M., Shirahata, A., and Kamio, Y., Covalent linkage of polyamines to peptidoglycan in Anaerovibrio lipolytica. J. Bacteriol., 182, 1154-1157 (2000).
7. Takatsuka, Y., Onoda, M., Sugiyama, T., Muramoto, K., Tomita, T., and Kamio, Y., Novel characteristics of Selenomonas ruminantium lysine decarboxylase capable of decarboxylating both l-lysine and L-ornithine. Biosci. Biotechnol. Biochem., 63, 1063-1069 (1999).
8. Takatsuka, Y., Yamaguchi, Y., Ono, M., and Kamio, Y., Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes. J. Bacteriol., 182, 6732-6741 (2000).
9. Takatsuka, Y., Tomita, T., and Kamio, Y., Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase. Biosci. Biotechnol. Biochem., 63, 1843-1846 (1999).
10. Hayashi, S., Murakami, Y., and Matsufuji, S., Ornithine decarboxylase antizyme: a novel type of regulatory protein. Trans Biochem. Sci., 21, 27-30 (1996).