+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

The Mtr2-Mex67 NTF2-like domain complex. Structural insights into a dual role of Mtr2 for yeast nuclear export

The Mtr2-Mex67 NTF2-like domain complex. Structural insights into a dual role of Mtr2 for yeast nuclear export

Journal of Biological Chemistry 278(48): 48395-48403

The formation of the Mtr2-Mex67 heterodimer is essential for yeast mRNA export as it constitutes a key nuclear component for shuttling mRNA between the nuclear and cytoplasm compartments through the nuclear pore complex. We report the crystal structures of apo-Mtr2 from the human pathogen Candida albicans and of its complex with the Mex67 NTF2-like domain. Compared with other members of the NTF2 fold family, Mtr2 displays novel structural features involved in the nuclear export of the large ribosomal subunit and consistent with a dual functional role of Mtr2 during yeast nuclear export events. The structure of the Mtr2-Mex67 NTF2-like domain complex, which overall is similar to those of the human and Saccharomyces cerevisiae homologs, unveils three putative Phe-Gly repeat binding sites, of which one contributes to the heterodimer interface. These structures exemplify an unrecognized adaptability of the NTF2 building block in evolution, identify novel structural determinants associated with key biological functions at the molecular surface of the yeast Mtr2-Mex67 complex, and suggest that the yeast and human mRNA export machineries may differ.

Please choose payment method:

(PDF emailed within 0-6 h: $19.90)

Accession: 012630753

Download citation: RISBibTeXText

PMID: 14504280

DOI: 10.1074/jbc.m308275200

Related references

Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2. Structure 23(7): 1246-1257, 2015

Role of Mex67-Mtr2 in the nuclear export of 40S pre-ribosomes. Plos Genetics 8(8): E1002915, 2012

Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface. Nucleic Acids Research 43(3): 1927-1936, 2015

Nuclear export of ribosomal 60S subunits by the general mRNA export receptor Mex67-Mtr2. Molecular Cell 26(1): 51-62, 2007

Sharing the load: Mex67-Mtr2 cofunctions with Los1 in primary tRNA nuclear export. Genes and Development 31(21): 2186-2198, 2017

Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum. Acta Crystallographica. Section F Structural Biology Communications 71(Pt 7): 876-888, 2015

The nuclear mRNA export receptor Mex67-Mtr2 of Trypanosoma brucei contains a unique and essential zinc finger motif. Molecular Microbiology 88(4): 728-739, 2013

A versatile interaction platform on the Mex67-Mtr2 receptor creates an overlap between mRNA and ribosome export. Embo Journal 27(1): 6-16, 2007

Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15. EMBO Reports 4(7): 699-703, 2003

Nuclear mRNA accumulation causes nucleolar fragmentation in yeast mtr2 mutant. Molecular Biology of the Cell 5(11): 1253-1263, 1994

Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor. Molecular Cell 8(3): 645-656, 2001

Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats. Journal of Biological Chemistry 284(26): 17575-17583, 2009

MTR2, an essential nuclear protein which affects mRNA transport and the distribution of nucleolar components in Saccharomyces cerevisiae. Molecular Biology of the Cell 4(Suppl. ): 83A, 1993

Conserved nuclear export sequences in Schizosaccharomyces pombe Mex67 and human TAP function in mRNA export by direct nuclear pore interactions. Journal of Biological Chemistry 279(17): 17434-17442, 2004

NTF2-like domain of Tap plays a critical role in cargo mRNA recognition and export. Nucleic Acids Research 43(3): 1894-1904, 2015