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PMID: 7904267 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification of an AU-rich RNA binding protein from Sarcophaga peregrina (flesh fly) and its identification as a Thiolase.

Journal of biochemistry ·Vol. 114 ·No. 3 ·1993-09-00 ·Pages 432-7

Nanbu R, Kubo T, Hashimoto T, Natori S

Abstract

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.

MeSH Terms
Acetyl-CoA C-Acetyltransferase/analysis Adenine/analysis Amino Acid Sequence Animals Base Composition/physiology Base Sequence Diptera/enzymology Molecular Sequence Data RNA-Binding Proteins/chemistry,isolation & purification Sequence Homology, Amino Acid Uracil/analysis
Chemicals
RNA-Binding Proteins Uracil Acetyl-CoA C-Acetyltransferase Adenine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Nanbu R
Faculty of Pharmaceutical Sciences, University of Tokyo.
Kubo T
Hashimoto T
Natori S
Article Info
Journal
Journal of biochemistry
Abbr.
J Biochem
ISSN
0021-924X
Published
1993-09-00
Pages
432-7
Language
English
Region
England
NLM ID
0376600
Subset
IM
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