MISC

基本情報

氏名 古賀 雄一
氏名(カナ) コガ ユウイチ
氏名(英語) Koga Yuuichi
所属 工学部 応用化学科
職名 教授
researchmap研究者コード 5000076449
researchmap機関 岡山理科大学

題名

Structural, thermodynamic, and mutational analyses of a psychrotrophic RNase HI.

単著・共著の別

 

著者

Takashi Tadokoro
Dong-Ju You
Yumi Abe
Hyongi Chon
Hiroyoshi Matsumura
Yuichi Koga
Kazufumi Takano
Shigenori Kanaya

概要

Ribonuclease (RNase) HI from the psychrotrophic bacterium Shewanella oneidensis MR-1 was overproduced in Escherichia coli, purified, and structurally and biochemically characterized. The amino acid sequence of MR-1 RNase HI is 67% identical to that of E. coli RNase HI. The crystal structure of MR-1 RNase HI determined at 2.0 A resolution was highly similar to that of E. coli RNase HI, except that the number of intramolecular ion pairs and the fraction of polar surface area of MR-1 RNase HI were reduced compared to those of E. coli RNase HI. The enzymatic properties of MR-1 RNase HI were similar to those of E. coli RNase HI. However, MR-1 RNase HI was much less stable than E. coli RNase HI. The stability of MR-1 RNase HI against heat inactivation was lower than that of E. coli RNase HI by 19 degrees C. The conformational stability of MR-1 RNase HI was thermodynamically analyzed by monitoring the CD values at 220 nm. MR-1 RNase HI was less stable than E. coli RNase HI by 22.4 degrees C in Tm and 12.5 kJ/mol in DeltaG(H2O). The thermodynamic stability curve of MR-1 RNase HI was characterized by a downward shift and increased curvature, which results in an increased DeltaCp value, compared to that of E. coli RNase HI. Site-directed mutagenesis studies suggest that the difference in the number of intramolecular ion pairs partly accounts for the difference in stability between MR-1 and E. coli RNases HI.

発表雑誌等の名称

Biochemistry

出版者

AMER CHEMICAL SOC

46

25

開始ページ

7460

終了ページ

8

発行又は発表の年月

2007-06-26

査読の有無

無し

依頼の有無

無し

記述言語

英語

掲載種別

 

ISSN

 

ID:DOI

10.1021/bi7001423

ID:NAID(CiNiiのID)

 

ID:PMID

 

JGlobalID

 

arXiv ID

 

ORCIDのPut Code

 

DBLP ID