PURIFICATION OF AN AU-RICH RNA-BINDING PROTEIN FROM SARCOPHAGA-PEREGRINA (FLESH FLY) AND ITS IDENTIFICATION AS A THIOLASE

被引:38
|
作者
NANBU, R [1 ]
KUBO, T [1 ]
HASHIMOTO, T [1 ]
NATORI, S [1 ]
机构
[1] SHINSHU UNIV,FAC MED,MATSUMOTO,NAGANO 390,JAPAN
来源
JOURNAL OF BIOCHEMISTRY | 1993年 / 114卷 / 03期
关键词
D O I
10.1093/oxfordjournals.jbchem.a124193
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 results suggest that the RNA binding activity is an intrinsic character of thiolase.
引用
收藏
页码:432 / 437
页数:6
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