Identification of sirtuin and its target as the ribosomal protein S4 in <i>Lactobacillus paracasei</i>
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- Atarashi Hotaka
- Department of Food and Cosmetic Science, Graduate School of Bioindustry, Tokyo University of Agriculture
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- Kawasaki Shinji
- Department of Bioscience, Tokyo University of Agriculture
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- Niimura Yoichi
- Department of Bioscience, Tokyo University of Agriculture
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- Tanaka Naoto
- Culture Collection Center, NODAI Research Institute, Tokyo University of Agriculture
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- Okada Sanae
- Culture Collection Center, NODAI Research Institute, Tokyo University of Agriculture
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- Shiwa Yuh
- Genome Research Center, NODAI Research Institute, Tokyo University of Agriculture Division of Biobank and Data management, Iwate Tohoku Medical Megabank Organization, Iwate Medical University
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- Endo Akihito
- Department of Food and Cosmetic Science, Graduate School of Bioindustry, Tokyo University of Agriculture
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- Nakagawa Junichi
- Department of Food and Cosmetic Science, Graduate School of Bioindustry, Tokyo University of Agriculture
抄録
Sirtuin is a protein with an enzymatic activity of NAD+-dependent protein deacetylation. It was first identified in yeast and its homologous genes have been widely found in various organisms. In bacteria, sirtuin gene was first described as cobB, encoding a cobalamin processing enzyme; and later its potential involvement in regulating acetylation levels of metabolic enzymes, transcription factors, chemotactic proteins and others have been reported. In order to study its physiological relevance in probiotic lactic acid bacteria, we analyzed the whole genome of three L. paracasei strains. All strains tested had sirtuin homolog genes designated hereby as sirA, and one of them had an additional gene designated as sirB. Following confirmation of their coding sequences by individual gene cloning, corresponding recombinant proteins have been generated and purified. The enzymatic characterization revealed that the intrinsic NAD+-dependent deacetylation activity of LpSirA (protein encoded by sirA) is comparable to human SIRT1. Furthermore, by blocking sirtuin activity using nicotinamide in vivo, together with an in vitro deacetylation reaction using recombinant LpSirA, we identified one of the target proteins in the lactic acid bacteria as the 30S ribosomal protein S4 (rpsD product).
収録刊行物
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- The Journal of General and Applied Microbiology
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The Journal of General and Applied Microbiology 62 (2), 98-105, 2016
公益財団法人 応用微生物学・分子細胞生物学研究奨励会