One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers

FEBS Letters

Klug, Gabriele¹  Evguenieva-Hackenberg, Elena¹  Conrad, Christian¹  Schmitt, Jens Guido¹ 

[1] Institut für Mikro- und Molekularbiologie der Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 26–32, D-35392 Giessen, Germany

关键词: RNase III;    Heterodimer;    RNA processing;    Dimeric enzyme;   

DOI  :  10.1016/S0014-5793(02)02653-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To study the intersubunit communication required for the activity of the normally homodimeric enzyme endoribonuclease III of Escherichia coli we have constructed and analysed an artificial heterodimer. This heterodimer is composed of one wild-type and one catalytically inactive subunit. The inactive subunit has one amino acid exchanged (E117K, rnc70 mutant) which abolishes cleavage activity but still allows substrate binding of a rnc70-homodimer. Our results show that one functional active site is sufficient for cleavage activity of the heterodimer.

【 授权许可】

Unknown