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Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface

DOI: 10.1093/nar/gkv030 DOI Help
PMID: 25618852 PMID Help

Authors: Shintaro Aibara (MRC Laboratory of Molecular Biology) , Eugene Valkov (MRC Laboratory of Molecular Biology, Cambridge, U.K.) , Meindert Lamers (MRC Laboratory of Molecular Biology) , M. Stewart (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research , VOL 43 (3) , PAGES 1927 - 1936

State: Published (Approved)
Published: February 2015
Diamond Proposal Number(s): 8547

Open Access Open Access

Abstract: The Mex67:Mtr2 complex is the principal yeast nuclear export factor for bulk mRNA and also contributes to ribosomal subunit export. Mex67 is a modular protein constructed from four domains (RRM, LRR, NTF2-like and UBA) that have been thought to be joined by flexible linkers like beads on a string, with the RRM and LRR domains binding RNAs and the NTF2-like and UBA domains binding FG-nucleoporins to facilitate movement through nuclear pores. Here, we show that the NTF2-like domain from Saccharomyces cerevisiae Mex67:Mtr2 also contributes to RNA binding. Moreover, the 3.3 Å resolution crystal structure of the Mex67ΔUBA:Mtr2 complex, supplemented with small angle X-ray scattering data, indicated that the LRR domain has a defined spatial relationship to the Mex67NTF2L:Mtr2 region. Conversely, the RRM domain and especially the UBA domain are more mobile. The conformation assumed by the LRR and NTF2-like domains results in clusters of positively-charged residues on each becoming arranged to form a continuous interface for binding RNA on the opposite side of the complex to the region that interacts with FG-nucleoporins to facilitate passage through nuclear pores.

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: ESRF

Added On: 19/03/2015 14:04

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