The DNA-binding domain in the Bacillus subtilis transition-state regulator AbrB employs significant motion for promiscuous DNA recognition. Academic Article uri icon

Overview

MeSH

  • Amino Acid Sequence
  • Bacterial Proteins
  • Binding Sites
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Motion
  • Nucleic Acid Conformation
  • Pliability
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Static Electricity
  • Substrate Specificity
  • Thermodynamics

MeSH Major

  • Bacillus subtilis
  • DNA
  • DNA-Binding Proteins
  • Transcription Factors

abstract

  • AbrB is a Bacillus subtilis protein responsible for regulating a diverse array of unrelated genes during periods of sub-optimal growth conditions. DNA binding by AbrB is unique in that sequence recognition is specific, yet no obvious consensus sequence of bound promoter regions is apparent. The N-terminal domain is a recently characterized representative of a novel class of DNA-binding proteins that possess a looped-hinge helix DNA-binding topology. Although the structural characterization of this DNA-binding topology contributed to an understanding of the architectural basis for recognition of DNA target sequences, specific mechanisms responsible for promiscuity in DNA sequence recognition still were not apparent. Analysis of (15)N backbone relaxation parameters shows that dynamic motion of regions directly linked to DNA binding show concerted motion on the microsecond-millisecond timescale. Furthermore, dynamic motion of the hinge region suggests that the DNA-binding region is capable of conformational orientations that allow it to accommodate DNA sequence variability in the cognate binding sites. Copyright 2001 Academic Press.

publication date

  • January 19, 2001

has subject area

  • Amino Acid Sequence
  • Bacillus subtilis
  • Bacterial Proteins
  • Binding Sites
  • DNA
  • DNA-Binding Proteins
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Motion
  • Nucleic Acid Conformation
  • Pliability
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Static Electricity
  • Substrate Specificity
  • Thermodynamics
  • Transcription Factors

Research

keywords

  • Journal Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1006/jmbi.2000.4305

PubMed ID

  • 11152601

Additional Document Info

start page

  • 429

end page

  • 439

volume

  • 305

number

  • 3