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Hyperreactivity of adenines and conformational flexibility of a translational repression site
Author(s) -
Talbot Simon J.,
Medina Gloria,
Fishwick Colin W.G.,
Haneef I.,
Stockley Peter G.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80576-o
Subject(s) - divalent , chemistry , stereochemistry , posttranslational modification , reagent , flexibility (engineering) , reactivity (psychology) , biochemistry , enzyme , medicine , organic chemistry , statistics , alternative medicine , mathematics , pathology
We have used a diethylpyrocarbonate (DEPC) modification [(1976) Prog. Nucl. Acids Res. 16, 189–262] to probe the accessibility of adenines essential for coat protein binding in the MS2 translational operator [(1983) Biochemistry 22, 2601–2610, 2610–2615, 4723–4730; (1987) Biochemistry 26, 1563–1568]. The essential adenines are apparently hyperreactive with this reagent relative to other sites within the same molecule. Variation of ionic strength, pH and divalent cation concentrations reveal the existence of two distinct conformers of the RNA operator as judged by DEPC reactivity. We propose that the hyperreactivity observed is due to the participation of neighbouring bases in the DEPC modification reaction and can be used as a novel structural probe.