Biophysical properties of regions flanking the bHLH-Zip motif in the p22 Max protein

Sharon E. Pursglove, Malin Fladvad, Massimo Bellanda, Ahmad Moshref, Marie Henriksson, Jannette Carey, Maria Sunnerhagen

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

The Max protein is the central dimerization partner in the Myc-Max-Mad network of transcriptional regulators, and a founding structural member of the family of basic-helixa-loop-helix (bHLH)-leucine zipper (Zip) proteins. Biologically important regions flanking its bHLH-Zip motif have been disordered or absent in crystal structures. The present study shows that these regions are resistant to proteolysis in both the presence and absence of DNA, and that Max dimers containing both flanking regions have significantly higher helix content as measured by circular dichroism than that predicted from the crystal structures. Nuclear magnetic resonance measurements in the absence of DNA also support the inferred structural order. Deletion of both flanking regions is required to achieve maximal DNA affinity as measured by EMSA. Thus, the previously observed functionalities of these Max regions in DNA binding, phosphorylation, and apoptosis are suggested to be linked to structural properties.

Original languageEnglish (US)
Pages (from-to)750-759
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume323
Issue number3
DOIs
StatePublished - Oct 22 2004

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Keywords

  • Binding
  • Chymotrypsin
  • Circular dichroism
  • Denaturation
  • EMSA
  • Limited proteolysis
  • NMR
  • Transcriptional regulator

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