Hyperreactivity of adenines and conformational flexibility of a translational repression site

Simon Talbot; G Medina; C W Fishwick; I Haneef; P G Stockley

Hyperreactivity of adenines and conformational flexibility of a translational repression site

Simon Talbot, G Medina, C W Fishwick, I Haneef, P G Stockley

Deanery of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	159-64
Number of pages	6
Journal	FEBS Letters
Volume	283
Issue number	1
Publication status	Published - 1991

Keywords / Materials (for Non-textual outputs)

Adenine
Bacteriophages
Base Sequence
Capsid
Diethyl Pyrocarbonate
Electrophoresis, Polyacrylamide Gel
Molecular Sequence Data
Nucleic Acid Conformation
Plasmids
Protein Biosynthesis
RNA
Transcription, Genetic

Cite this

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title = "Hyperreactivity of adenines and conformational flexibility of a translational repression site",

abstract = "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.",

keywords = "Adenine, Bacteriophages, Base Sequence, Capsid, Diethyl Pyrocarbonate, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Nucleic Acid Conformation, Plasmids, Protein Biosynthesis, RNA, Transcription, Genetic",

author = "Simon Talbot and G Medina and Fishwick, {C W} and I Haneef and Stockley, {P G}",

year = "1991",

language = "English",

volume = "283",

pages = "159--64",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Hyperreactivity of adenines and conformational flexibility of a translational repression site

AU - Talbot, Simon

AU - Medina, G

AU - Fishwick, C W

AU - Haneef, I

AU - Stockley, P G

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

KW - Adenine

KW - Bacteriophages

KW - Base Sequence

KW - Capsid

KW - Diethyl Pyrocarbonate

KW - Electrophoresis, Polyacrylamide Gel

KW - Molecular Sequence Data

KW - Nucleic Acid Conformation

KW - Plasmids

KW - Protein Biosynthesis

KW - RNA

KW - Transcription, Genetic

M3 - Article

C2 - 1709880

SN - 0014-5793

VL - 283

SP - 159

EP - 164

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Hyperreactivity of adenines and conformational flexibility of a translational repression site

Abstract

Keywords / Materials (for Non-textual outputs)

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