Raghunathan P L, Guthrie C
University of California, San Francisco, School of Medicine, Department of Biochemistry and Biophysics, San Francisco, CA 94143-0448, USA.
Science. 1998 Feb 6;279(5352):857-60. doi: 10.1126/science.279.5352.857.
The spliceosome removes introns from pre-messenger RNAs by a mechanism that entails extensive remodeling of RNA structure. The most conspicuous rearrangement involves disruption of 24 base pairs between U4 and U6 small nuclear RNAs (snRNAs). Here, the yeast RNA binding protein Prp24 is shown to reanneal these snRNAs. When Prp24 is absent, unpaired U4 and U6 small nuclear ribonucleoprotein particles (snRNPs) accumulate; with time, splicing becomes inhibited. Addition of purified Prp24 protein regenerates duplex U4/U6 snRNPs for new rounds of splicing. The reannealing reaction catalyzed by Prp24 proceeds more efficiently with snRNPs than with deproteinized snRNAs.
剪接体通过一种需要对RNA结构进行广泛重塑的机制从前体信使RNA中去除内含子。最显著的重排涉及U4和U6小核RNA(snRNA)之间24个碱基对的破坏。在这里,酵母RNA结合蛋白Prp24被证明能使这些snRNA重新退火。当没有Prp24时,未配对的U4和U6小核糖核蛋白颗粒(snRNP)会积累;随着时间的推移,剪接会受到抑制。添加纯化的Prp24蛋白可使双链U4/U6 snRNP再生,用于新一轮的剪接。Prp24催化的重新退火反应在snRNP上比在脱蛋白的snRNA上进行得更有效。