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A LexA mutant repressor with a relaxed inter-domain linker

P Oertel-Buchheit1, J Reinbolt, M John

  • 1Institut de Biologie Moléculaire et Cellulaire, UPR 9002 du CNRS, Strasbourg, France.

Protein Science : a Publication of the Protein Society
|April 1, 1998
PubMed
Summary

The LexA protein

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Area of Science:

  • Molecular Biology
  • Protein Structure
  • Biochemistry

Background:

  • LexA protein belongs to prokaryotic transcriptional repressors.
  • It has DNA binding and dimerization domains separated by a hinge region.
  • The hinge region is widely considered flexible and unconstrained.

Purpose of the Study:

  • To investigate the structural flexibility of the LexA protein's hinge region.
  • To challenge the prevailing hypothesis of a fully flexible inter-domain linker.

Main Methods:

  • Utilized a mutant LexA repressor with point mutations in the hinge region.
  • Assessed protease sensitivity (trypsin and Glu-C) of the wild-type and mutant LexA hinge regions.

Main Results:

  • Mutant LexA hinge region showed sensitivity to protease cleavage over a 20-amino acid segment.
  • Wild-type LexA hinge region demonstrated resistance to the same proteases.
  • These findings contradict the notion of a completely flexible linker.

Conclusions:

  • The LexA hinge region is not entirely flexible and is likely constrained.
  • Constrained structure may result from interactions with the carboxy-terminal domain or intrinsic local stability.

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