Uridylation and adenylation of RNAs
- PMID: 26563174
- PMCID: PMC5089844
- DOI: 10.1007/s11427-015-4954-9
Uridylation and adenylation of RNAs
Abstract
The posttranscriptional addition of nontemplated nucleotides to the 3' ends of RNA molecules can have a significant impact on their stability and biological function. It has been recently discovered that nontemplated addition of uridine or adenosine to the 3' ends of RNAs occurs in different organisms ranging from algae to humans, and on different kinds of RNAs, such as histone mRNAs, mRNA fragments, U6 snRNA, mature small RNAs and their precursors etc. These modifications may lead to different outcomes, such as increasing RNA decay, promoting or inhibiting RNA processing, or changing RNA activity. Growing pieces of evidence have revealed that such modifications can be RNA sequence-specific and subjected to temporal or spatial regulation in development. RNA tailing and its outcomes have been associated with human diseases such as cancer. Here, we review recent developments in RNA uridylation and adenylation and discuss the future prospects in this research area.
Keywords: U6 snRNA; Uridylation; adenylation; histone mRNA; miRNA; pre-miRNA; rRNA.
Conflict of interest statement
The authors declare that they have no conflict of interest.
Figures



References
-
- Sprinzl M, Cramer F. The-CCA end of tRNA and its role in protein biosynthesis. Proc Natl Acad Sci USA. 1979;22:1–69. - PubMed
-
- Scott DD, Norbury CJ. RNA decay via 3′ uridylation. Biochim Biophys Acta. 2013;1829:654–665. - PubMed
-
- Wickens M, Kwak JE. A tail tale for U. Science. 2008;319:1344–1345. - PubMed
-
- Wang Z-F, Whitfield ML, Ingledue TCr, Dominski Z, Marzluff WF. The protein that binds the 3′ end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing. Genes Dev. 1996;10:3028–3040. - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources