Nanbu R, Kubo T, Hashimoto T, Natori S
Faculty of Pharmaceutical Sciences, University of Tokyo.
J Biochem. 1993 Sep;114(3):432-7. doi: 10.1093/oxfordjournals.jbchem.a124193.
A protein that binds to the AU-rich sequence in the 3'-untranslated region of sarcotoxin IIA mRNA was purified from a Sarcophaga pupal extract to near homogeneity. The molecular mass of this protein was estimated to be 39 kDa by SDS-polyacrylamide gel electrophoresis. The partial amino acid sequences of two peptides obtained from the 39 kDa protein showed striking similarities to partial amino acid sequences of rat and yeast 3-oxoacyl-CoA thiolase, suggesting that this protein is a Sarcophaga thiolase. In fact, the purified 39 kDa protein was found to have thiolase activity. Moreover, rat mitochondrial 3-oxoacyl-CoA thiolase showed affinity to the AU-rich RNA. These suggest that the RNA binding activity is an intrinsic character of thiolase.
从麻蝇蛹提取物中纯化出一种与肌毒素IIA mRNA 3'-非翻译区富含AU序列结合的蛋白质,纯度接近均一。通过SDS-聚丙烯酰胺凝胶电泳估计该蛋白质的分子量为39 kDa。从39 kDa蛋白质获得的两个肽段的部分氨基酸序列与大鼠和酵母3-氧代酰基辅酶A硫解酶的部分氨基酸序列有显著相似性,表明该蛋白质是麻蝇硫解酶。事实上,纯化的39 kDa蛋白质被发现具有硫解酶活性。此外,大鼠线粒体3-氧代酰基辅酶A硫解酶对富含AU的RNA有亲和力。这些表明RNA结合活性是硫解酶的固有特性。