Identification of gemin5 as a novel 7-methylguanosine cap-binding protein.

ABSTRACT:

Background

A unique attribute of RNA molecules synthesized by RNA polymerase II is the presence of a 7-methylguanosine (m(7)G) cap structure added co-transcriptionally to the 5' end. Through its association with trans-acting effector proteins, the m(7)G cap participates in multiple aspects of RNA metabolism including localization, translation and decay. However, at present relatively few eukaryotic proteins have been identified as factors capable of direct association with m(7)G.

Methodology/principal findings

Employing an unbiased proteomic approach, we identified gemin5, a component of the survival of motor neuron (SMN) complex, as a factor capable of direct and specific interaction with the m(7)G cap. Gemin5 was readily purified by cap-affinity chromatography in contrast

SUBMITTER: Bradrick SS 

PROVIDER: S-EPMC2736588 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature