Publications by authors named "Ivaylo D Yonchev"

Article Synopsis
  • RBMXL2, a nuclear protein specific to germ cells, represses cryptic splicing during meiosis and is crucial for male fertility, while its similar counterpart RBMX regulates splicing in somatic cells.
  • RBMX interacts with long exons and helps maintain genome stability by preventing the use of harmful splice sites, complementing the gene silencing that occurs during male meiosis.
  • Both RBMX and RBMXL2 share parallel functions across somatic and germline tissues, suggesting their roles in splicing have been evolutionarily conserved for over 200 million years.
View Article and Find Full Text PDF

Despite the nuclear localization of the mA machinery, the genomes of multiple exclusively-cytoplasmic RNA viruses, such as chikungunya (CHIKV) and dengue (DENV), are reported to be extensively mA-modified. However, these findings are mostly based on mA-Seq, an antibody-dependent technique with a high rate of false positives. Here, we address the presence of mA in CHIKV and DENV RNAs.

View Article and Find Full Text PDF

The epitranscriptomic modification -methyladenosine (mA) is a ubiquitous feature of the mammalian transcriptome. It modulates mRNA fate and dynamics to exert regulatory control over numerous cellular processes and disease pathways, including viral infection. Kaposi's sarcoma-associated herpesvirus (KSHV) reactivation from the latent phase leads to the redistribution of mA topology upon both viral and cellular mRNAs within infected cells.

View Article and Find Full Text PDF

-methyladenosine (mA) is the most abundant internal RNA modification of cellular mRNAs. mA is recognised by YTH domain-containing proteins, which selectively bind to mA-decorated RNAs regulating their turnover and translation. Using an mA-modified hairpin present in the Kaposi's sarcoma associated herpesvirus (KSHV) RNA, we identified seven members from the 'Royal family' as putative mA readers, including SND1.

View Article and Find Full Text PDF