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PDBsum entry 5eim
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RNA binding protein/RNA
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PDB id
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5eim
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DOI no:
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Biochem Biophys Res Commun
491:310-316
(2017)
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PubMed id:
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Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1.
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B.Wu,
J.Xu,
S.Su,
H.Liu,
J.Gan,
J.Ma.
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ABSTRACT
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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.
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');
}
}
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