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Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15
Author(s) -
Fribourg Sébastien,
Conti Elena
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.embor883
Subject(s) - rna , nuclear export signal , biology , messenger rna , rna binding protein , genetics , protein subunit , microbiology and biotechnology , structural similarity , peptide sequence , homology (biology) , gene , biochemistry
The association between Mtr2 and Mex67 is essential for the nuclear export of bulk messenger RNA in yeast. In metazoans, the analogous function is carried out by the TAP–p15 heterodimer. Whereas Mex67 and TAP are highly conserved proteins, their binding partners, Mtr2 and p15, share no sequence similarity, but are nevertheless functionally homologous. Here, we report the 2.8‐Å resolution crystal structure of Mtr2 in complex with the NTF2‐like domain of Mex67. Mtr2 is a novel member of the NTF2‐like family and interacts with Mex67, forming a complex with a similar structural architecture to that of TAP–p15. Mtr2 fulfils an analogous function to that of human p15 in maintaining the structural integrity of the heterodimer. In addition, Mtr2 presents a long internal loop, which contains residues that affect the export of the large ribosomal subunit.