A dual role of divalent metal ions in catalysis and folding of RNase H1 from extreme halophilic archaeon Halobacterium sp. NRC-1

FEBS Open Bio

Volumn 2, Issue , 2012, Pages 345-352

  Tannous, Elias ^a   Yokoyama, Koji ^a   You, Dong Ju ^a,b   Koga, Yuichi ^a   Kanaya, Shigenori ^a  

^a OSAKA UNIVERSITY   (Japan)

^b Korea Basic Science Institute (KBSI)   (South Korea)

Author keywords

Divalent metal ions; Halobacterium sp. NRC 1; N terminal domain; RNase H; Salt dependent folding

Indexed keywords

RIBONUCLEASE H;

ARTICLE; BACTERIAL STRAIN; CATALYSIS; ENZYME ACTIVE SITE; ENZYME DENATURATION; ENZYME STRUCTURE; HALOBACTERIUM; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

ARCHAEA; HALOBACTERIUM SP. NRC-1;

EID: 84868347674     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2012.10.003     Document Type: Article

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