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NikR is a ribbon-helix-helix DNA-binding protein

Published online by Cambridge University Press:  01 November 1999

PETER T. CHIVERS
Affiliation:
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
ROBERT T. SAUER
Affiliation:
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
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Abstract

Escherichia coli NikR, a repressor with homologs in other bacteria and archaea, was identified as a potential new member of the ribbon-helix-helix (β-α-α) family of transcription factors in profile based sequence searches and in structure prediction experiments. Biophysical and biochemical characterization of the N-terminal domain of NikR show that it has many features expected of a β-α-α protein including α-helical content, dimeric solution form, concentration dependent thermal stability, and ability to bind DNA in sequence-specific manner. Mutation of a residue predicted to be important for DNA-binding reduces operator affinity but does not affect the secondary structure or stability of the protein.

Type
Research Article
Copyright
© 1999 The Protein Society

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