Biophysical properties of regions flanking the bHLH-Zip motif in the p22 Max protein
2004 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, Vol. 323, no 3, 750-759 p.Article in journal (Refereed) Published
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-helix-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.
Place, publisher, year, edition, pages
2004. Vol. 323, no 3, 750-759 p.
binding; denaturation; EMSA; limited proteolysis; NMR; chymotrypsin; transcriptional regulator; circular dichroism
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-53517DOI: 10.1016/j.bbrc.2004.08.166OAI: oai:DiVA.org:liu-53517DiVA: diva2:289684