2MZS

NMR structure of the RRM2 domain of Hrb1

Summary for 2MZS

• Entry DOI: 10.2210/pdb2mzs/pdb
• Related: 2MZQ 2MZR 2MZT
• NMR Information: BMRB: 25498
• Descriptor: Protein HRB1 (1 entity in total)
• Functional Keywords: rrm, rna binding domain, hrb1, tho/trex, rna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus : P38922
• Total number of polymer chains: 1
• Total formula weight: 10701.63

Authors

Martinez-Lumbreras, S.,Seraphin, B.,Perez-Canadillas, J. (deposition date: 2015-02-23, release date: 2015-12-02, Last modification date: 2024-05-15)

Primary citation

Martinez-Lumbreras, S.,Taverniti, V.,Zorrilla, S.,Seraphin, B.,Perez-Canadillas, J.M.
Gbp2 interacts with THO/TREX through a novel type of RRM domain.
Nucleic Acids Res., 44:437-448, 2016

PubMed Abstract: 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.

PubMed: 26602689
DOI: 10.1093/nar/gkv1303

Experimental method

SOLUTION NMR