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首页> 外文期刊>Molecular and Cellular Biology >A dominant negative mutation in a spliceosomal ATPase affects ATP hydrolysis but not binding to the spliceosome.
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A dominant negative mutation in a spliceosomal ATPase affects ATP hydrolysis but not binding to the spliceosome.

机译：剪接体ATPase中的显性负突变影响ATP水解，但不与剪接体结合。

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PRP16 is an RNA-dependent ATPase required for the second catalytic step of splicing in vitro. A dominant suppressor of a branchpoint mutation in Saccharomyces cerevisiae, the prp16-1 allele, contains a Tyr to Asp change in the nucleotide-binding site consensus sequence. We now find that cells harboring the prp16-1 allele have a general growth defect that is exacerbated at cold temperatures. The mutant is dominant over the wild-type gene when overexpressed. Purified Prp16-1 protein binds to the spliceosome with apparently wild-type affinity; however, it only weakly complements the second-step block in a PRP16-depleted extract. Analysis of purified Prp16-1 revealed that the rate of ATP hydrolysis is greatly reduced. These results can account for the dominant negative growth phenotype and argue that the ATPase activity of PRP16 is essential for its role in splicing. Moreover, since PRP16 is a member of the DEAD/H box families, these findings have important implications for a large class of proteins.
机译：PRP16是第二种体外剪接催化步骤所需的RNA依赖性ATPase。酿酒酵母中分支点突变的主要抑制因子prp16-1等位基因在核苷酸结合位点共有序列中包含从Tyr到Asp的变化。现在我们发现，带有prp16-1等位基因的细胞具有一般的生长缺陷，在低温下会加剧这种缺陷。当过表达时，突变体在野生型基因上占优势。纯化的Prp16-1蛋白以明显的野生型亲和力与剪接体结合。但是，它仅对补充PRP16的提取物中的第二步程序进行了微弱的补充。对纯化的Prp16-1的分析表明，ATP水解的速率大大降低了。这些结果可以解释显性负增长表型，并认为PRP16的ATPase活性对其剪接作用至关重要。此外，由于PRP16是DEAD / H box家族的成员，因此这些发现对一大类蛋白质具有重要意义。

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