PT  - JOURNAL ARTICLE
AU  - Wu, Baixing
AU  - Xu, Jinhao
AU  - Su, Shichen
AU  - Liu, Hehua
AU  - Gan, Jianhua
AU  - Ma, Jinbiao
TI  - Structural basis for the specific recognition of DSR by the YTH domain containing protein Mmi1
AID  - 10.1101/145276
DP  - 2017 Jan 01
TA  - bioRxiv
PG  - 145276
4099  - http://biorxiv.org/content/early/2017/06/02/145276.short
4100  - http://biorxiv.org/content/early/2017/06/02/145276.full
AB  - Meiosis is one of the most dramatic differentiation programs accompanied by a striking change in gene expression profiles, whereas a number of meiosis-specific transcripts are expressed untimely in mitotic cells. The entry of meiosis will be blocked as the accumulation of meiosis-specific mRNAs during the mitotic cell in fission yeast Schizosaccharomyces pombe. 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 contain a conservative motif 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 YTH domain of Mmi1 binds to high-affinity RNA targets r(A1U2U3A4A5A6C7A8) containing DSR core motif. 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 function although it has a similar fold as other ones.