High impact information on REC107

• A genetic selection was devised to recover second-site mutations that bypass the requirement for MER1 in MER2 RNA-splicing [1].
• The suppressor mutation affects the first residue in U1 snRNA, allowing this nucleotide to base pair with the eighth nucleotide in the MER2 intron [1].
• The MER2 gene is transcribed in mitosis as well as meiosis; however, the transcript is spliced efficiently to generate a functional gene product only in meiosis [2].
• The MER2 gene product is essential for meiosis [3].
• This work defines a yeast splicing enhancer and shows that constitutively expressed and cell type-specific factors combine to regulate splicing of a specific subset of pre-mRNAs including SPO70, MER2, and MER3 [4].

Biological context of REC107

• This paper presents data to confirm that two of them, REC102 and REC107, are general, meiosis-specific recombination genes that have no detectable role during mitosis [5].
• Deficiency of recombination in a mre2 mutant that has an amino acid substitution in the N-terminal RRM can be suppressed by the MER2 gene on the multicopy plasmid [6].
• If DSB formation is blocked (e.g., by a spo11 mutation), dephosphorylation of Mer2 and its dissociation from chromosomes are delayed [7].
• Mer2 localizes to distinct foci on meiotic chromosomes, with foci maximally abundant prior to the formation of synaptonemal complex [7].
• The Mer2 protein is present in vegetative cells, but it increases in abundance and becomes phosphorylated specifically during meiotic prophase [7].

Associations of REC107 with chemical compounds

• Translation of IME1 has been proposed to occur only in meiotic cells; several meiotic transcripts are more stable in acetate medium than in glucose medium; and splicing of MER2 RNA depends on a meiosis-specific gene, MER1 [8].

Physical interactions of REC107

• Thus, Mer1 interacts directly with a regulatory element in MER2 RNA and promotes splicing [9].

Co-localisations of REC107

• We have also found that the Mei4 and Rec114 proteins localize to foci on chromosomes and these foci partially colocalize with each other and with Mer2 [7].

Regulatory relationships of REC107

• A gene called MER2 partially suppresses the mer1 phenotype when present in high copy number [3].

Other interactions of REC107

• Further analysis showed that the Mre2 protein is involved in meiosis-specific splicing of the MER2 transcripts in cooperation with the Mer1 protein [6].
• We propose that Mer2, Mei4, and Rec114 form a distinct complex required for DSB formation [7].
• Therefore, at least one of the functions of the MER1 protein is to mediate splicing of the MER2 transcript [2].

Analytical, diagnostic and therapeutic context of REC107

• Sequence analysis and genetic complementation indicate that REC107 is identical to the MER2 gene [5].
• The Mer1 protein contains the KH motif found in some RNA-binding proteins, and RNA gel mobility shift assays demonstrate that Mer1 binds specifically to MER2 RNA [9].
• Fluorescence in situ hybridization of chromosome-specific DNA probes to spread meiotic chromosomes demonstrates that homolog alignment is also significantly reduced in the mer2 mutant [10].
• In addition, mer2 abolishes intrachromosomal meiotic recombination, both in the ribosomal DNA array and in an artificial duplication [10].

References