Researchers
- KATO Akinori
- Associate Professor
Faculty | Department of Advanced Bioscience / Graduate School of Agriculture |
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Researchmap | https://researchmap.jp/read0137572 |
Research Activities
Research Areas
- Life sciences, Bacteriology
- Life sciences, Molecular biology
- Life sciences, Systems genomics
- Life sciences, Genomics
Research Interests
比較ゲノム, 情報伝達, 遺伝子発現調節, Comparative genomics, Signal transduction, Gene regulation
Published Papers
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Development of conjugation-mediated versatile site-specific single-copy luciferase fusion system
Akinori Kato
The Journal of General and Applied Microbiology 69 (6) , 318-326, May. 2024 , Refereed -
Isolation and draft genome sequence of Enterobacter asburiae strain i6 amenable to genetic manipulation
Akinori Kato
Journal of Genomics 12 , 26-34, Jan. 2024 , Refereed -
Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control.
Yoshitani K; Ishii E; Taniguchi K; Sugimoto H; Shiro Y; Akiyama Y; Kato A; Utsumi R; Eguchi Y
Bioscience, biotechnology, and biochemistry 83 (4) , 684-694, Apr. 2019 , Refereed
MISC
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Reciprocal Control between a Bacterium's Regulatory System and the Modification Status of Its Lipopolysaccharide
, Akinori Kato; H. Deborah Chen; Tammy Latifi; Eduardo A. Groisman , MOLECULAR CELL , 47 , 6 , 897 , 908 , Sep. 2012
Summary:Gram-negative bacteria often modify their lipopolysaccharide (LPS), thereby increasing resistance to antimicrobial agents and avoidance of the host immune system. However, it is unclear how bacteria adjust the levels and activities of LPS-modifying enzymes in response to the modification status of their LPS. We now address this question by investigating the major regulator of LPS modifications in Salmonella enterica. We report that the PmrA/PmrB system controls expression of a membrane peptide that inhibits the activity of LpxT, an enzyme responsible for increasing the LPS negative charge. LpxT's inhibition and the PmrA-dependent incorporation of positively charged L-4-aminoarabinose into the LPS decrease Fe3+ binding to the bacterial cell. Because Fe3+ is an activating ligand for the sensor PmrB, transcription of PmrA-dependent LPS-modifying genes is reduced. This mechanism enables bacteria to sense their cell surface by its effect on the availability of an inducing signal for the system regulating cell-surface modifications. - Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor , A Kato, EA Groisman , Faculty Opinions , Sep. 2004
Research Grants & Projects
- Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for Young Scientists (A), Evolution of cross-regulatory profiles of two-component signal transduction systems among closely related bacterial pathogens , 近畿大学
- Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for Young Scientists (Start-up), Elucidation of connector-mediated regulatory networks controlling Bacterial virulence , 近畿大学