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Journal of Bacteriology, January 2008, p. 442-446, Vol. 190, No. 1
0021-9193/08/$08.00+0     doi:10.1128/JB.01429-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Two Segments in Bacterial Antizyme P22 Are Essential for Binding and Enhance Degradation of Lysine/Ornithine Decarboxylase in Selenomonas ruminantium{triangledown}

Yoshihiro Yamaguchi,1,{dagger} Yumiko Takatsuka,1,{ddagger} and Yoshiyuki Kamio2*

Laboratory of Applied Microbiology, Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan,1 Department of Human Health and Nutrition, Graduate School of Comprehensive Human Sciences, Shokei Gakuin University, Yurigaoka 4-10-1, Natori 981-1295, Japan2

Received 4 September 2007/ Accepted 18 October 2007

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.

* Corresponding author. Mailing address: Department of Human Health and Nutrition, Graduate School of Comprehensive Human Sciences, Shokei Gakuin University, Yurigaoka 4-10-1, Natori 981-1295, Japan. Phone and fax: 81-22-381-3347. E-mail: ykamio{at}shokei.ac.jp

{triangledown} Published ahead of print on 26 October 2007.

{dagger} Present address: Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854.

{ddagger} Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202.

Journal of Bacteriology, January 2008, p. 442-446, Vol. 190, No. 1
0021-9193/08/$08.00+0     doi:10.1128/JB.01429-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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