Comparative Analyses of Hairpin Substrate Recognition byEscherichia coliandBacillus subtilisRibonuclease P Ribozymes | Zendy

Tomoaki Ando | Zendy; Terumichi Tanaka | Zendy; Yo Kikuchi | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Comparative Analyses of Hairpin Substrate Recognition byEscherichia coliandBacillus subtilisRibonuclease P Ribozymes

Author(s) -

Tomoaki Ando,

Terumichi Tanaka,

Yo Kikuchi

Publication year - 2003

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.67.1825

Subject(s) - ribozyme , bacillus subtilis , rnase p , escherichia coli , ribonuclease , substrate (aquarium) , rna , rnase h , biochemistry , chemistry , vs ribozyme , hairpin ribozyme , magnesium , ribonuclease iii , biology , bacteria , organic chemistry , genetics , ecology , gene , rna interference

Previously, we reported that the substrate shape recognition of the Escherichia coli ribonuclease (RNase) P ribozyme depends on the concentration of magnesium ion in vitro. We additionally examined the Bacillus subtilis RNase P ribozyme and found that the B. subtilis enzyme also required high magnesium ion, above 10 mM, for cleavage of a hairpin substrate. The results of kinetic studies showed that the metal ion concentration affected both the catalysis and the affinity of the ribozymes toward a hairpin RNA substrate.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research