Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published August 1995 | public
Journal Article

Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATp

Abstract

The transcription factor AP-1 activates the expression of numerous genes in response to mitogenic stimuli. AP-1 regulates gene expression both through solitary binding to independent recognition sites and, in cooperation with various heterologous transcription factors, through targeting to composite response elements. The two subunits that make up the AP-1 heterodimer, Fos and Jun, possess identical residues at positions that make sequence-specific contacts to DNA. This degeneracy leaves the protein with no apparent way of orienting itself uniquely on DNA by differentially recognizing its two non-identical half-sites. Here, we have analyzed the orientation of the AP-1 basic-leucine-zipper (bZip) domain on a cognate site, both alone and in the cooperative complex formed together with the 'nuclear factor of activated T cells' (NFATp).

Additional Information

© 1995 Elsevier Science Ltd. Received 27 March 1995, Revised 5 June 1995, Accepted 6 June 1995. This work was supported by grants (to G.L.V. and A.R.) from Hoffmann-La Roche (Institute of Chemistry and Medicine) and (to P.B.D.) National Institutes of Health (GM-27681). M.G.O was partially supported by a predoctoral fellowship from the National Science Foundation. We thank Steve Harrison for discussions and for sharing the coordinates of the Fos-Jun co-complex prior to publication.

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023