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XB-ART-27885
FEBS Lett 1987 Nov 02;2232:232-6.
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Thesaurin a, the major protein of Xenopus laevis previtellogenic oocytes, present in the 42 S particles, is homologous to elongation factor EF-1 alpha.

Viel A , Djé MK , Mazabraud A , Denis H , le Maire M .


Abstract
We have purified in SDS X.laevis thesaurin a (Mr 50,000) which is part of the 42 S storage particles. Its N-terminal amino acid is blocked and several peptides obtained by V8 protease treatment were purified and sequenced. As expected from one of the functional roles of the 42 S particles (tRNA binding, protection against deacylation and exchange with the ribosome), the amino acid sequence of thesaurin a was found to be closely related to that of the elongation factor EF-1 alpha. We suggest that all three proteins involved in 5 S RNA and tRNA storage in previtellogenic oocytes, TFIIIA, thesaurin a and thesaurin b, have a dual function: storage and a role in transcription or in protein synthesis.

PubMed ID: 3666148
Article link: FEBS Lett


Species referenced: Xenopus laevis
Genes referenced: 42sp43 42sp50 eef1a1 gtf3a mt-tr trna