Structural highlights
Function
[RL7A_ARCFU] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA and box C/D sRNAs.[1]
Publication Abstract from PubMed
N(6)-methyladenine is the most common covalent modification in cellular RNA species, with demonstrated functional consequences. At the molecular level this methylation could alter local RNA structure, and/or modulate the binding of specific proteins. We have previously shown that trans-Hoogsteen-sugar (sheared) A:G base pairs can be completely disrupted by methylation, and that this occurs in a sub-set ofD/D k-turn structures. In this work we have investigated to what extent sequence context affects the severity with which inclusion of N(6)-methyladenine into different A:G base pairs of a standard k-turn affects RNA folding and L7Ae protein binding. We find that local sequence has a major influence, ranging from complete absence of folding and protein binding to a relatively mild effect. We have determined the crystal structure of one of these species both free and protein-bound, showing the environment of the methyl group and the way the modification is accommodated into the k-turn structure.
Effect of methylation of adenine N(6) on kink turn structure depends on location.,Ashraf S, Huang L, Lilley DMJ RNA Biol. 2019 Jun 24:1-9. doi: 10.1080/15476286.2019.1630797. PMID:31234702[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rozhdestvensky TS, Tang TH, Tchirkova IV, Brosius J, Bachellerie JP, Huttenhofer A. Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaea. Nucleic Acids Res. 2003 Feb 1;31(3):869-77. PMID:12560482
- ↑ Ashraf S, Huang L, Lilley DMJ. Effect of methylation of adenine N(6) on kink turn structure depends on location. RNA Biol. 2019 Jun 24:1-9. doi: 10.1080/15476286.2019.1630797. PMID:31234702 doi:http://dx.doi.org/10.1080/15476286.2019.1630797