Purification of an AU-rich RNA binding protein from Sarcophaga peregrina (flesh fly) and its identification as a Thiolase.
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.
Nanbu
R
R
Faculty of Pharmaceutical Sciences, University of Tokyo.
Kubo
T
T
Hashimoto
T
T
Natori
S
S
D000101:Acetyl-CoA C-Acetyltransferase / Q000032:analysis*; D000225:Adenine / Q000032:analysis*; D000595:Amino Acid Sequence; D000818:Animals; D001482:Base Composition / Q000502:physiology; D001483:Base Sequence; D004175:Diptera / Q000201:enzymology*; D008969:Molecular Sequence Data; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D014498:Uracil / Q000032:analysis*
D016601:RNA-Binding Proteins; D014498:Uracil; D000101:Acetyl-CoA C-Acetyltransferase; D000225:Adenine