6EXZ
Crystal structure of Mex67 C-term
Summary for 6EXZ
Entry DOI | 10.2210/pdb6exz/pdb |
Descriptor | mRNA export factor MEX67, FORMIC ACID (3 entities in total) |
Functional Keywords | mrna export, transport protein |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Total number of polymer chains | 1 |
Total formula weight | 8333.55 |
Authors | Mohamad, N.,Bravo, J. (deposition date: 2017-11-10, release date: 2018-11-21, Last modification date: 2024-01-17) |
Primary citation | Martin-Exposito, M.,Gas, M.E.,Mohamad, N.,Nuno-Cabanes, C.,Tejada-Colon, A.,Pascual-Garcia, P.,de la Fuente, L.,Chaves-Arquero, B.,Merran, J.,Corden, J.,Conesa, A.,Perez-Canadillas, J.M.,Bravo, J.,Rodriguez-Navarro, S. Mip6 binds directly to the Mex67 UBA domain to maintain low levels of Msn2/4 stress-dependent mRNAs. Embo Rep., :e47964-e47964, 2019 Cited by PubMed Abstract: RNA-binding proteins (RBPs) participate in all steps of gene expression, underscoring their potential as regulators of RNA homeostasis. We structurally and functionally characterize Mip6, a four-RNA recognition motif (RRM)-containing RBP, as a functional and physical interactor of the export factor Mex67. Mip6-RRM4 directly interacts with the ubiquitin-associated (UBA) domain of Mex67 through a loop containing tryptophan 442. Mip6 shuttles between the nucleus and the cytoplasm in a Mex67-dependent manner and concentrates in cytoplasmic foci under stress. Photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation experiments show preferential binding of Mip6 to mRNAs regulated by the stress-response Msn2/4 transcription factors. Consistent with this binding, MIP6 deletion affects their export and expression levels. Additionally, Mip6 interacts physically and/or functionally with proteins with a role in mRNA metabolism and transcription such as Rrp6, Xrn1, Sgf73, and Rpb1. These results reveal a novel role for Mip6 in the homeostasis of Msn2/4-dependent transcripts through its direct interaction with the Mex67 UBA domain. PubMed: 31680439DOI: 10.15252/embr.201947964 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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