Hostname: page-component-78c5997874-fbnjt Total loading time: 0 Render date: 2024-11-11T05:44:04.678Z Has data issue: false hasContentIssue false

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
Get access

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)