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DNA binding properties of the purified Antennapedia homeodomain

Affolter, M. and Percival-Smith, A. and Muller, M. and Leupin, W. and Gehring, W. J.. (1990) DNA binding properties of the purified Antennapedia homeodomain. Proceedings of the National Academy of Sciences of the United States of America, Vol. 87, H. 11. pp. 4093-4097.

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Official URL: http://edoc.unibas.ch/dok/A5258974

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Abstract

The in vitro DNA binding properties of a purified 68-amino acid Antennapedia homeodomain (Antp HD) peptide have been analyzed. Equilibrium and kinetic binding studies showed that stable DNA-protein complexes are formed with a Kd of 1.6 x 10(-9) M and 1.8 x 10(-10) M, respectively. Heterodimer analysis led to the conclusion that Antp HD interacts in vitro as a monomer with the DNA target sites used in our study. The results of methylation and ethylation interference studies indicated that the Antp HD closely approaches the target DNA primarily from one side in a region extending across three phosphate backbones. The DNA binding properties of the Antp HD and prokaryotic DNA binding domains that share a helix-turn-helix motif are compared.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Cell Biology (Affolter)
05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Gehring)
UniBasel Contributors:Gehring, Walter Jakob and Affolter, Markus
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:National Academy of Sciences
ISSN:0027-8424
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:14 Sep 2012 06:49
Deposited On:22 Mar 2012 13:21

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