U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

mmi1 YTH family RNA-binding protein Mmi1 [ Schizosaccharomyces pombe (fission yeast) ]

Gene ID: 2539540, updated on 18-Sep-2024

Summary

Go to the top of the page Help
Official Symbol
mmi1
Official Full Name
YTH family RNA-binding protein Mmi1
Primary source
PomBase:SPCC736.12c
Locus tag
SPOM_SPCC736.12C
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Schizosaccharomyces pombe (strain: 972h-)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See mmi1 in Genome Data Viewer
Location:
chromosome: III
Exon count:
5
Sequence:
Chromosome: III; NC_003421.2 (337088..340112, complement)

Chromosome III - NC_003421.2Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene argonaute Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene dehydrogenase Neighboring gene ncRNA Neighboring gene ncRNA

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_003421.2

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. Stowell JAW, et al. J Biol Chem, 2018 Jun 15. PMID 29695507, Free PMC Article
  2. Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1. Wu B, et al. Biochem Biophys Res Commun, 2017 Sep 16. PMID 28735863
  3. A novel RNA-binding mode of the YTH domain reveals the mechanism for recognition of determinant of selective removal by Mmi1. Wang C, et al. Nucleic Acids Res, 2016 Jan 29. PMID 26673708, Free PMC Article
  4. A scaffold lncRNA shapes the mitosis to meiosis switch. Andric V, et al. Nat Commun, 2021 Feb 3. PMID 33536434, Free PMC Article
  5. Inactivation of fission yeast Erh1 de-represses pho1 expression: evidence that Erh1 is a negative regulator of prt lncRNA termination. Schwer B, et al. RNA, 2020 Oct. PMID 32546512, Free PMC Article

See all (44) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
    Title: Meiotic gene silencing complex MTREC/NURS recruits the nuclear exosome to YTH-RNA-binding protein Mmi1.
  2. 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.
    Title: YTH-RNA-binding protein prevents deleterious expression of meiotic proteins by tethering their mRNAs to nuclear foci.
  3. 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.
    Title: mmi1 and rep2 mRNAs are novel RNA targets of the Mei2 RNA-binding protein during early meiosis in Schizosaccharomyces pombe.
  4. 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.
    Title: A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing.
  5. 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.
    Title: A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding.
  6. 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.
    Title: Ubiquitination-dependent control of sexual differentiation in fission yeast.
  7. 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.
    Title: Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1.
  8. 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
    Title: 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.
  9. 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.
    Title: Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.
  10. Mmi1 YTH domain selectively recognizes the determinant of selective removal RNA motif.
    Title: A novel RNA-binding mode of the YTH domain reveals the mechanism for recognition of determinant of selective removal by Mmi1.
Submit: New GeneRIF Correction See all GeneRIFs (12)

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by PomBase

Function Evidence Code Pubs
enables CCR4-NOT complex binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables N6-methyladenosine-containing RNA reader activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables RNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables lncRNA binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables mRNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables mRNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables pre-mRNA binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables pre-mRNA intronic binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein-RNA adaptor activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein-RNA adaptor activity IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in lncRNA catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in mRNA destabilization IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in nuclear RNA surveillance IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nuclear lncRNA surveillance IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nuclear mRNA surveillance of mRNA 3'-end processing IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nuclear mRNA surveillance of spliceosomal pre-mRNA splicing IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nuclear polyadenylation-dependent CUT catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of siRNA-independent facultative heterochromatin formation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulatory ncRNA 3'-end processing EXP
Inferred from Experiment
more info
 PubMed 
involved_in regulatory ncRNA-mediated gene silencing EXP
Inferred from Experiment
more info
 PubMed 
involved_in siRNA-independent facultative heterochromatin formation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
part_of Mei2 nuclear dot complex IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in chromatin IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in heterochromatin island IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in nuclear exosome focus IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in nucleus EXP
Inferred from Experiment
more info
 PubMed 
is_active_in nucleus HDA PubMed 
is_active_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
YTH family RNA-binding protein Mmi1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003421.2 Reference assembly

    Range
    337088..340112 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001022776.4 → NP_587783.2  YTH family RNA-binding protein Mmi1 [Schizosaccharomyces pombe]

    See identical proteins and their annotated locations for NP_587783.2

    Status: PROVISIONAL

    UniProtKB/Swiss-Prot
    O74958
    Conserved Domains (1) summary
    pfam04146
    Location:350 → 477
    YTH; YT521-B-like domain
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases
Research Materials