title: Two segments in bacterial antizyme P22 are essential for binding and enhance degradation of lysine/ornithine decarboxylase in Selenomonas ruminantium.
abstract: In Selenomonas ruminantium, a strictly anaerobic and gram-negative bacterium, the degradation of lysine/ornithine decarboxylase (LDC/ODC) by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain. Amino acid sequence alignment of S. ruminantium P22 with the L10 ribosomal proteins of gram-positive and -negative bacteria showed that P22 has a 5-residue K101NKLD105 segment and an 11-residue G160VIRNAVYVLD170 segment, both of which are lacking in L10 in any other gram-positive and gram-negative bacteria reported. To elucidate whether the two segments are involved in P22 function, a series of mutant genes of P22 were constructed and expressed in Escherichia coli. The proteins were isolated and assayed for their function with respect to S. ruminantium LDC/ODC and mouse ODC. The results indicated that the two segments of P22 are crucial for P22 binding to both enzymes and also accelerated degradation of both decarboxylases.
authors.affiliation: Laboratory of Applied Microbiology, Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan.
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Yamaguchi
authors.forename: Yumiko
authors.initials: Y
authors.lastname: Takatsuka
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Kamio
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D017931:DNA Primers; D004791:Enzyme Inhibitors / Q000378:metabolism*; D007700:Kinetics; D009955:Ornithine Decarboxylase / Q000378:metabolism*; D065108:Ornithine Decarboxylase Inhibitors; D010447:Peptide Hydrolases / Q000378:metabolism; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D020357:Selenomonas / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D017931:DNA Primers; D004791:Enzyme Inhibitors; D065108:Ornithine Decarboxylase Inhibitors; D011994:Recombinant Proteins; D012269:Ribosomal Proteins; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases; D002262:Carboxy-Lyases; D009955:Ornithine Decarboxylase; C021520:lysine decarboxylase