Purification and characterisation of cathepsin B mRNA 3'-untranslated-region-binding protein (CBBP), a protein that represses cathepsin B mRNA translation

Tamaki Yano, Ayako Kobayashi, Shoichiro Kurata, Shunji Natori

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

We reported that the 3'-untranslated region (3'-UTR) of cathepsin B mRNA of Sarcophaga peregrina (flesh fly) is necessary for the repression of its translation, and detected the 3'-UTR-binding protein in lysates of larval hemocytes in which cathepsin B mRNA translation was repressed [Yano, T., Kurata, S. and Natori, S. (1995) Eur. J. Biochem. 234, 39-43]. In this study, we purified the 3'-UTR-binding protein from an embryonic cell line of Sarcophaga. The purified protein (CBBP) was found to repress cathepsin B mRNA translation in a rabbit reticulocyte lysate. We found that the CBBP contents of the hemocytes did not change during metamorphosis, although the cathepsin B mRNA became translatable only at the pupal stage. Moreover, we found that pupal, but not larval hemocytes, contained a factor that inhibited the binding of CBBP to the 3'-UTR. A regulatory mechanism of cathepsin B expression in Sarcophaga hemocytes is discussed.

Original languageEnglish
Pages (from-to)260-265
Number of pages6
JournalEuropean Journal of Biochemistry
Volume245
Issue number2
DOIs
Publication statusPublished - 1997

Keywords

  • 3'-untranslated region
  • Cathepsin B
  • RNA-binding protein
  • Translocation regulation

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Purification and characterisation of cathepsin B mRNA 3'-untranslated-region-binding protein (CBBP), a protein that represses cathepsin B mRNA translation'. Together they form a unique fingerprint.

Cite this