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PDBsum entry 2mzr
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RNA binding protein
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PDB id
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2mzr
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References listed in PDB file
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Key reference
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Title
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Gbp2 interacts with tho/trex through a novel type of rrm domain.
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Authors
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S.Martínez-Lumbreras,
V.Taverniti,
S.Zorrilla,
B.Séraphin,
J.M.Pérez-Cañadillas.
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Ref.
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Nucleic Acids Res, 2016,
44,
437-448.
[DOI no: ]
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PubMed id
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Abstract
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Metazoan SR and SR-like proteins are important regulatory factors in RNA
splicing, export, translation and RNA decay. We determined the NMR structures
and nucleic acid interaction modes of Gbp2 and Hrb1, two paralogous budding
yeast proteins with similarities to mammalian SR proteins. Gbp2 RRM1 and RRM2
recognise preferentially RNAs containing the core motif GGUG. Sequence
selectivity resides in a non-canonical interface in RRM2 that is highly related
to the SRSF1 pseudoRRM. The atypical Gbp2/Hrb1 C-terminal RRM domains (RRM3) do
not interact with RNA/DNA, likely because of their novel N-terminal extensions
that block the canonical RNA binding interface. Instead, we discovered that RRM3
is crucial for interaction with the THO/TREX complex and identified key residues
essential for this interaction. Moreover, Gbp2 interacts genetically with Tho2
as the double deletion shows a synthetic phenotype and preventing Gbp2
interaction with the THO/TREX complex partly supresses gene expression defect
associated with inactivation of the latter complex. These findings provide
structural and functional insights into the contribution of SR-like proteins in
the post-transcriptional control of gene expression.
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