Premium
Thesaurin a, the major protein of Xenopus laevis previtellogenic oocytes, present in the 42 S particles, is homologous to elongation factor EF‐1α
Author(s) -
Viel Alain,
Djé Marcellin K.,
Mazabraud André,
Denis Herman,
le Maire Marc
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80295-8
Subject(s) - eukaryotic translation elongation factor 1 alpha 1 , xenopus , elongation factor , storage protein , elongation , amino acid , homologous chromosome , transfer rna , protein biosynthesis , rna , biology , ribosome , chemistry , microbiology and biotechnology , biochemistry , gene , materials science , ultimate tensile strength , metallurgy
We have purified in SDS X. laevis thesaurin a ( M r 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‐1α. 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.