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Effect of methylation of adenine N6 on kink turn structure depends on location
DOI:
10.1080/15476286.2019.1630797
Authors:
Saira
Ashraf
(Cancer Research UK Nucleic Acid Structure Research Group, The University of Dundee)
,
Lin
Huang
(Cancer Research UK Nucleic Acid Structure Research Group, The University of Dundee)
,
David
Lilley
(Cancer Research UK Nucleic Acid Structure Research Group, The University of Dundee)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Rna Biology
State:
Published (Approved)
Published:
June 2019

Abstract: N6-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 N6-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.
Journal Keywords: RNA structure; RNA methylation; epigenetic modification; N6-methyladenine; kink-turn; X-ray crystallography
Subject Areas:
Biology and Bio-materials,
Chemistry
Instruments:
I03-Macromolecular Crystallography
Added On:
03/07/2019 10:29
Documents:
bnhh44.pdf
Discipline Tags:
Biochemistry
Chemistry
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)