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Can the Monomer of the Leucine Zipper Proteins Recognize the Dimer Binding Site without Dimerization?

Park, Changmoon and Campbell, Judy L. and Goddard, William A., III (1996) Can the Monomer of the Leucine Zipper Proteins Recognize the Dimer Binding Site without Dimerization? Journal of the American Chemical Society, 118 (18). pp. 4235-4239. ISSN 0002-7863. http://resolver.caltech.edu/CaltechAUTHORS:20170408-133818781

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Abstract

It is generally believed that leucine zipper regulatory proteins for DNA transcription recognize their DNA binding sites as dimers preformed in solution (and that the monomers do not bind specifically to these sites). To test this idea, we synthesized the 31-residue peptide v-Jun-br, which contains only the DNA binding region of the v-Jun monomer. Footprinting assays show that v-Jun-br monomers specifically protect the DNA binding site of v-Jun in almost identically the same way as dimers. Thus, (i) the monomer recognizes the half-site of the dimer binding site and (ii) dimerization does not appreciably affect the bound conformation of each monomer. These results may have implications in the regulation of transcription by such proteins. Thus, two monomers of v-Jun might bind sequentially to the dimer binding site followed by dimerization of v-Jun while bound. This may allow binding at concentrations too low for dimerization in solution.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/ja950653tDOIArticle
http://pubs.acs.org/doi/abs/10.1021/ja950653tPublisherArticle
ORCID:
AuthorORCID
Goddard, William A., III0000-0003-0097-5716
Additional Information:© 1996 American Chemical Society. Received February 27, 1995. Revised Manuscript Received October 12, 1995. This research was supported by a grant from the Biological and Chemical Technology Research (BCTR) Program (David Boron) of the Department of Energy. The facilities of the Materials and Molecular Simulation Center (MSC) are also supported by grants from the National Science Foundation (CHE 94-13930 and ASC 92-17368), Asahi Chemical, Asahi Glass, Chevron Petroleum Technology Co., BF Goodrich, BP Chemical, Vestar, Hughes Research Laboratories, Xerox, and Beckman Institute.
Funders:
Funding AgencyGrant Number
Department of Energy (DOE)UNSPECIFIED
NSFCHE 94-13930
NSFASC 92-17368
Asahi ChemicalUNSPECIFIED
Asahi GlassUNSPECIFIED
Chevron Petroleum Technology Co.UNSPECIFIED
BF GoodrichUNSPECIFIED
BP ChemicalUNSPECIFIED
VestarUNSPECIFIED
Hughes Research LaboratoriesUNSPECIFIED
XeroxUNSPECIFIED
Caltech Beckman InstituteUNSPECIFIED
Record Number:CaltechAUTHORS:20170408-133818781
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20170408-133818781
Official Citation:Can the Monomer of the Leucine Zipper Proteins Recognize the Dimer Binding Site without Dimerization? Changmoon Park, Judy L. Campbell, and William A. Goddard, III Journal of the American Chemical Society 1996 118 (18), 4235-4239 DOI: 10.1021/ja950653t
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:75872
Collection:CaltechAUTHORS
Deposited By: 1Science Import
Deposited On:13 Apr 2017 20:18
Last Modified:13 Apr 2017 20:18

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