Green C J, Rivera-León R, Vold B S
SRI International, Menlo Park, CA 94025-3493, USA.
Nucleic Acids Res. 1996 Apr 15;24(8):1497-503. doi: 10.1093/nar/24.8.1497.
A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the Km, indicating that the deleted structures may be important for binding to the precursor tRNA substrate but not for the cleavage reaction. Under some reaction conditions, this RNase P deletion mutant can become a relatively non-specific nuclease, indicating that this RNA's catalytic center may be more exposed. The catalytic core of the RNase P is formed by less than one third of the 377 residues of the RNase P RNA.
大肠杆菌核糖核酸酶P催化RNA组分缺失87 - 241位残基的缺失突变体保留了与蛋白质组分相互作用以形成功能性催化剂的能力。这一系统发育保守区域的缺失显著增加了米氏常数(Km),表明缺失的结构可能对与前体tRNA底物的结合很重要,但对切割反应不重要。在某些反应条件下,这种核糖核酸酶P缺失突变体可成为一种相对非特异性的核酸酶,表明该RNA的催化中心可能更暴露。核糖核酸酶P的催化核心由核糖核酸酶P RNA的377个残基中不到三分之一的残基形成。