RT Journal Article
SR Electronic
T1 Structural basis for the specific recognition of DSR by the YTH domain containing protein Mmi1
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 145276
DO 10.1101/145276
A1 Wu, Baixing
A1 Xu, Jinhao
A1 Su, Shichen
A1 Liu, Hehua
A1 Gan, Jianhua
A1 Ma, Jinbiao
YR 2017
UL http://biorxiv.org/content/early/2017/06/02/145276.abstract
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.