Purification of two thermostable components of messenger ribonucleoprotein particles (mRNPs) from Xenopus laevis oocytes, belonging to a novel class of RNA‐binding proteins

FEBS Letters

Denis, Herman¹  le Maire, Marc¹  Viel, Alain¹  Deschamps, Stéphane¹ 

[1] Centre de Gènètique molèculaire, Laboratoire propre du Centre National de la Recherche Scientifique, associéà l'Universitè P. et M. Curie (Paris VI), F-91 198 Gif-sur-Yvette Cedex, France

关键词: mRNA-containing particle;    mRNP;    Amino acid sequence;    Sequence homology;    Xenopus laevis;    Oogenesis;   

DOI  :  10.1016/0014-5793(91)80456-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have purified and partially sequenced two proteins from Xenopus laevis previtellogenic oocytes, belonging to messenger ribonucleoprotein particles (mRNPs). The purification procedure rests on the thermostability of these proteins, which remain soluble after heating the cell extracts at 80°C. The thermostable proteins can be identified with two of the most abundant components (mRNP3 and mRNP4) of the mRNPs, described by Darnbrough and Ford (1981) [Eur. J. Biochem. 118, 415–424]. mRNP3 and mRNP4 are homologous to each other, but to no other protein of known sequence. The abundance and semi-periodic distribution of proline residues in mRNF3 and mRNF4 sequences suggest that these RNA-binding proteins adopt an unusual type of conformation

【 授权许可】

Unknown