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PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs.

Abstract：

:Messenger RNAs produced by splicing are translated more efficiently than those produced from similar intronless precursor mRNAs (pre-mRNAs). The exon-junction complex (EJC) probably mediates this enhancement; however, the specific link between the EJC and the translation machinery has not been identified. The EJC proteins Y14 and magoh remain bound to spliced mRNAs after their export from the nucleus to the cytoplasm and are removed only when these mRNAs are translated. Here we show that PYM, a 29-kDa protein that binds the Y14-magoh complex in the cytoplasm, also binds, via a separate domain, to the small (40S) ribosomal subunit and the 48S preinitiation complex. Furthermore, PYM knockdown reduces the translation efficiency of a reporter protein produced from intron-containing, but not intronless, pre-mRNA. We suggest that PYM functions as a bridge between EJC-bearing spliced mRNAs and the translation machinery to enhance translation of the mRNAs.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Diem MD,Chan CC,Younis I,Dreyfuss G

doi

10.1038/nsmb1321

subject

Has Abstract

pub_date

2007-12-01 00:00:00

pages

1173-9

issue

12

eissn

1545-9993

issn

1545-9985

pii

nsmb1321

journal_volume

14

pub_type

杂志文章

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