PDBsum entry 2mzr

RNA binding protein

PDB id: 2mzr

Contents

Protein chain

95 a.a.

PDB id:

2mzr

Name:

RNA binding protein

Title:

Nmr structure of the rrm1 domain of hrb1

Structure:

Protein hrb1. Chain: a. Fragment: first rrm domain (unp residues 144-236). Synonym: protein tom34. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: hrb1, n2009, tom34, ynl004w. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

S.Martinez-Lumbreras,B.Seraphin,J.Perez-Canadillas

Key ref:

S.Martínez-Lumbreras et al. (2016). Gbp2 interacts with THO/TREX through a novel type of RRM domain. Nucleic Acids Res, 44, 437-448. PubMed id: 26602689 DOI: 10.1093/nar/gkv1303

Date:

23-Feb-15 Release date: 02-Dec-15

Protein chain

P38922  (HRB1_YEAST) -  Serine/arginine (SR)-type shuttling mRNA binding protein HRB1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 454 a.a.

Struc: 95 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gkv1303

Nucleic Acids Res 44:437-448 (2016)

PubMed id: 26602689

Gbp2 interacts with THO/TREX through a novel type of RRM domain.

S.Martínez-Lumbreras, V.Taverniti, S.Zorrilla, B.Séraphin, J.M.Pérez-Cañadillas.

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.