ニシヤマ ソウイチロウ
Soichiro Nishiyama
西山 宗一郎 所属 新潟薬科大学 応用生命科学部 応用生命科学科 職種 准教授 |
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言語種別 | 英語 |
発行・発表の年月 | 2014/01 |
形態種別 | 論文 |
査読 | 査読あり |
標題 | Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis. |
執筆形態 | 共著 |
掲載誌名 | Journal of bacteriology |
掲載区分 | 国外 |
巻・号・頁 | 196(2),pp.257-64 |
著者・共著者 | ◎Nishiyama So-ichiro, Garzón Andrés, Parkinson John S |
概要 | The histidine autokinase CheA functions as the central processing unit in the Escherichia coli chemotaxis signaling machinery. The CheA phosphorylation site, His-48, lies in the N-terminal P1 domain, which must engage the CheA ATP-binding domain, P4, to initiate an autophosphorylation reaction cycle. The docking determinants for the P1-P4 interaction have not been experimentally identified. One set of P1 mutants identified amino acid replacements at surface-exposed residues distal to His-48. These lesions reduced the rate of P1 transphosphorylation by P4. However, once phosphorylated, the mutant P1 domains transferred phosphate to CheY at the wild-type rate. Thus, these P1 mutants appear to define interaction determinants for P1-P4 docking during the CheA autophosphorylation reaction. |
DOI | 10.1128/JB.01167-13 |
ISSN | 1098-5530 |
PMID | 24163342 |