Minor groove-binding architectural proteins: structure, function, and DNA recognition

Annu Rev Biophys Biomol Struct. 1998;27:105-31. doi: 10.1146/annurev.biophys.27.1.105.

Abstract

To date, high-resolution structures have been solved for five different architectural proteins complexed to their DNA target sites. These include TATA-box-binding protein, integration host factor (IHF), high mobility group I(Y)[HMG I(Y)], and the HMG-box-containing proteins SRY and LEF-1. Each of these proteins interacts with DNA exclusively through minor groove contacts and alters DNA conformation. This paper reviews the structural features of these complexes and the roles they play in facilitating assembly of higher-order protein-DNA complexes and discusses elements that contribute to sequence-specific recognition and conformational changes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Binding Sites
  • DNA / chemistry*
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • HMGA1a Protein
  • High Mobility Group Proteins / chemistry
  • High Mobility Group Proteins / metabolism
  • Humans
  • Integration Host Factors
  • Models, Molecular
  • Nuclear Proteins*
  • Nucleic Acid Conformation*
  • Protein Conformation*
  • Sex-Determining Region Y Protein
  • TATA-Box Binding Protein
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism*

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • High Mobility Group Proteins
  • Integration Host Factors
  • Nuclear Proteins
  • SRY protein, human
  • Sex-Determining Region Y Protein
  • TATA-Box Binding Protein
  • Transcription Factors
  • HMGA1a Protein
  • DNA