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6EXZ

Crystal structure of Mex67 C-term

Summary for 6EXZ
Entry DOI10.2210/pdb6exz/pdb
DescriptormRNA export factor MEX67, FORMIC ACID (3 entities in total)
Functional Keywordsmrna export, transport protein
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Total number of polymer chains1
Total formula weight8333.55
Authors
Mohamad, N.,Bravo, J. (deposition date: 2017-11-10, release date: 2018-11-21, Last modification date: 2024-01-17)
Primary citationMartin-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: 31680439
DOI: 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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數據於2024-11-06公開中

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