Abstract
N1-methyladenosine (m1A) is a kind of common and abundant methylation modification in eukaryotic mRNA and long-chain non-coding RNA. Nucleoside methyltransferase (MTase) of m1A is a diverse protein family, which is characterized by the presence of methyltransferases like domains and conserved S-adenosylmethionine (SAM) binding domains formed by the central sevenstranded beta-sheet structure. However, comprehensive analysis of the gene expression profile of such enzymes has not been performed to classify them according to evolutionary criteria and to guide the functional prediction. Here, we conducted extensive searches of databases to collect all members of previously identified m1A RNA methyltransferases. And we report bioinformatics studies on gene expression profile based on evolutionary analysis, sequence alignment, expression in tissues and cells within the family of RNA methyltransferases. Our analysis showed that the base modification behavior mediated by m1A RNA methyltransferases evolved from invertebrate, and the active sites of m1A RNA methyltransferases were highly conserved during the evolution from invertebrates to human. And m1A RNA methyltransferases have low tissue and cell specificity.
Highlights
RNA is a key link between DNA and protein in the process of genetic information transmission, but the level of synthesized protein is not necessarily positively correlated with the level of mRNA, suggesting the importance of post-transcriptional modification of RNA1
Internal modification occurs in many types of RNA, of which N6-methyladenosine (m6A), the most common modification in eukaryotes, refers to methylation of adenylate at the sixth nitrogen position3. m1A modification is different from m6A in that it occurs on the first N atom of the adenine base group and has a positive charge under physiological conditions. m1A was first found in non-coding RNA such as rRNA and tRNA and widely existed in prokaryotic and eukaryotic mRNA4
M1A modification is related to translation initiation sites, and transcripts containing m1A have higher translation efficiency5. m1A is a positively charged nucleotide modification, and the methyl group on m1A will block the Watson-Crick base complementary pairing of adenine, which makes them have an important contribution to the formation of tRNA structure[6]
Summary
RNA is a key link between DNA and protein in the process of genetic information transmission, but the level of synthesized protein is not necessarily positively correlated with the level of mRNA, suggesting the importance of post-transcriptional modification of RNA1. Dominissini[5] and Li4 developed transcriptome-wide sequencing methods to identify and map m1A in mRNA These studies indicate that m1A is reversible and is mainly concentrated near the start codon of eukaryotic mRNA. There are a variety of RNA methyltransferases and demethylases in cells, as well as various methyl binding proteins. Under their combined action, different types of RNA undergo dynamic changes of methylation and demethylation to regulate various physiological processes. To understand the origin of these enzymes in detail, we summarized the species without m1A methyltransferase orthologues together with the corresponding discussion of the gene sequences and structure to verify the evolution of RNA methylation modifications. The results of the present studies provide a further understanding of the evolutionary profile of RNA modification and valuable insights into their functions
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