Interaction of S. pombe Mmi1 with the nuclear exosome is mediated by a complex termed MTREC (Mtl1-Red1 core) or NURS (nuclear RNA silencing) that is composed of a conserved zinc-finger protein, Red1, and an RNA helicase, Mtl1. Physical interaction between Mmi1 and the nuclear exosome depends on Red1. Study findings shed light on the target recognition mechanisms of post-transcriptional regulation. | Meiotic gene silencing complex MTREC/NURS recruits the nuclear exosome to YTH-RNA-binding protein Mmi1. Shichino Y, Otsubo Y, Yamamoto M, Yamashita A., Free PMC Article | 05/16/2020 |
The authors propose that nuclear foci formed by Mmi1 are not only the site of RNA degradation, but also of sequestration of meiotic transcripts from the translation machinery. | YTH-RNA-binding protein prevents deleterious expression of meiotic proteins by tethering their mRNAs to nuclear foci. Shichino Y, Otsubo Y, Kimori Y, Yamamoto M, Yamashita A., Free PMC Article | 08/12/2019 |
Study suggests that at meiotic initiation, Mei2 may sequester rep2 mRNA to help allow pre-meiotic S, and then may bind both meiRNA and mmi1 mRNA to inactivate Mmi1 at two levels, the protein level and also the mRNA level, allowing meiosis. | mmi1 and rep2 mRNAs are novel RNA targets of the Mei2 RNA-binding protein during early meiosis in Schizosaccharomyces pombe. Mukherjee K, Futcher B, Leatherwood J., Free PMC Article | 03/23/2019 |
Study discover that an important function of Mmi1 in promoting non-canonical transcription termination at meiotic genes, and in preventing lncRNAs from invading and repressing adjacent genes, is not dependent upon its association with Erh1. | A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing. Xie G, Vo TV, Thillainadesan G, Holla S, Zhang B, Jiang Y, Lv M, Xu Z, Wang C, Balachandran V, Shi Y, Li F, Grewal SIS., Free PMC Article | 02/23/2019 |
This study reports that an N-terminal extension in mmi1 that is proximal to the YTH domain enhances RNA binding. Using X-ray crystallography, NMR, and biophysical methods, the study shows that this low-complexity region in mmi1 becomes more ordered upon RNA binding. | A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. Stowell JAW, Wagstaff JL, Hill CH, Yu M, McLaughlin SH, Freund SMV, Passmore LA., Free PMC Article | 01/26/2019 |
The authors propose that Mmi1 recruits the Ccr4-Not complex to counteract its own inhibitor Mei2, thereby locking the system in a stable state that ensures the repression of the meiotic program by Mmi1. | Ubiquitination-dependent control of sexual differentiation in fission yeast. Simonetti F, Candelli T, Leon S, Libri D, Rougemaille M., Free PMC Article | 05/19/2018 |
Mmi1 can recognize and bind a class of meiosis-specific transcripts expressed inappropriately in mitotic cells; structural insights into the specific recognition of these mRNAs by the YTH domain containing protein Mmi1 have been presented. | Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1. Wu B, Xu J, Su S, Liu H, Gan J, Ma J. | 08/26/2017 |
report the 1.75 A crystal structure of the Mmi1 YTH domain and provide evidence that Mmi1 recognizes DSR RNA via a binding mode distinct from that of structurally homologous YTH proteins that recognize m(6)A-modified RNA | Transcription of lncRNA prt, clustered prt RNA sites for Mmi1 binding, and RNA polymerase II CTD phospho-sites govern the repression of pho1 gene expression under phosphate-replete conditions in fission yeast. Chatterjee D, Sanchez AM, Goldgur Y, Shuman S, Schwer B., Free PMC Article | 07/22/2017 |
Erh1 and the RNA-binding protein Mmi1 form a stoichiometric complex, called the Erh1-Mmi1 complex (EMC), to promote meiotic mRNA decay and facultative heterochromatin assembly. | Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly. Sugiyama T, Thillainadesan G, Chalamcharla VR, Meng Z, Balachandran V, Dhakshnamoorthy J, Zhou M, Grewal SIS., Free PMC Article | 07/30/2016 |
Mmi1 YTH domain selectively recognizes the determinant of selective removal RNA motif. | A novel RNA-binding mode of the YTH domain reveals the mechanism for recognition of determinant of selective removal by Mmi1. Wang C, Zhu Y, Bao H, Jiang Y, Xu C, Wu J, Shi Y., Free PMC Article | 06/28/2016 |
Mmi1 can specifically regulate the splicing of particular introns in a transcript: it inhibits the splicing of introns that are in the vicinity of putative Mmi1 binding sites, while allowing the splicing of other introns that are far from such sites. | The fission yeast RNA binding protein Mmi1 regulates meiotic genes by controlling intron specific splicing and polyadenylation coupled RNA turnover. Chen HM, Futcher B, Leatherwood J., Free PMC Article | 03/31/2012 |
Mei2 tethers Mmi1 and thereby stabilizes the transcripts necessary for the progression of meiosis | The selective elimination of messenger RNA underlies the mitosis-meiosis switch in fission yeast. Yamamoto M., Free PMC Article | 02/5/2011 |