5EIP

apo-structure of YTH domain of SpMmi1

Summary for 5EIP

• Entry DOI: 10.2210/pdb5eip/pdb
• Related: 5EIM
• Descriptor: YTH domain-containing protein mmi1 (2 entities in total)
• Functional Keywords: yth, mmi1, dsr, rna binding protein
• Biological source: Schizosaccharomyces pombe 972h- (Fission yeast)
• Cellular location: Nucleus : O74958
• Total number of polymer chains: 2
• Total formula weight: 30420.38

Authors

Wu, B.X.,Xu, J.H.,Su, S.C.,Ma, J.B. (deposition date: 2015-10-30, release date: 2016-01-27, Last modification date: 2024-03-20)

Primary citation

Wu, B.X.,Xu, J.H.,Su, S.C.,Liu, H.,Gan, J.,Ma, J.B.
Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1
Biochem. Biophys. Res. Commun., 491:310-316, 2017

PubMed Abstract: Meiosis is one of the most dramatic differentiation programs accompanied by a striking change in gene expression profiles in fission yeast Schizosaccharomyces pombe. Whereas a number of meiosis-specific transcripts are expressed untimely in mitotic cells, and the entry of meiosis will be blocked as the accumulation of meiosis-specific mRNAs in the mitotic cells. A YTH domain containing protein Mmi1 was identified as a pivotal effector in a post-transcriptional event termed selective elimination of meiosis-specific mRNAs. Mmi1 can recognize and bind a class of meiosis-specific transcripts expressed inappropriately in mitotic cells, which all contain a conservative region called DSR, as a mark to remove them in cooperation with nuclear exosomes. Here we report the 1.6 Å resolution crystal structure of the Mmi1-YTH domain in complex with a high consensus hexanucleotide motif, which is multiple copied in the DSR region. Our structure observations, supported by site-directed mutations of key residues illustrate the mechanism for specific recognition of DSR-RNA by Mmi1. Moreover, different from other YTH domain family proteins, Mmi1-YTH domain has a distinctive RNA-binding properties although it has a similar fold as other ones.

PubMed: 28735863
DOI: 10.1016/j.bbrc.2017.07.104

Experimental method

X-RAY DIFFRACTION (1.49 Å)