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Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving

Shin, Jumi A. and Ebright, Richard H. and Dervan, Peter B. (1991) Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving. Nucleic Acids Research, 19 (19). pp. 5233-5236. ISSN 0305-1048. PMCID PMC328881. https://resolver.caltech.edu/CaltechAUTHORS:20160510-145810397

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Abstract

Lac repressor (LacR) Is a helix-turn-helix motif sequence-specific DNA binding protein. Based on proton NMR spectroscopic investigations, Kaptein and co-workers have proposed that the hellx-turn-helix motif of LacR binds to DNA in an orientation opposite to that of the helix-turn-helix motifs of lambda; repressor, λ cro, 434 repressor, 434 cro, and CAP [Boelens, R., Scheek, R., van Boom, J. and Kaptein, R., J. Mol. Biol. 193, 1987, 213–216]. In the present work, we have determined the orientation of the hellx-turn-helix motif of LacR in the LacR-DNA complex by the affinity cleaving method. The DNA cleaving moiety EDTA-Fe was attached to the N-terminus of a 56-residue synthetic protein corresponding to the DNA binding domain of LacR. We have formed the complex between the modified protein and the left DNA half site for LacR. The locations of the resulting DNA cleavage positions relative to the left DNA half site provide strong support for the proposal of Kaptein and co-workers.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC328881/PubMed CentralArticle
http://dx.doi.org/10.1093/nar/19.19.5233DOIArticle
http://nar.oxfordjournals.org/content/19/19/5233.abstractPublisherArticle
Additional Information:© 1991 Oxford University Press. Received July 19, 1991; Revised and Accepted August 22, 1991. We are grateful to the DARPA University Research Initiative Program, Merck and Company, the Searle Scholars Program, and the National Science Foundation for support of this research. We are also grateful to the National Institute of General Medical Sciences for a Research Service Award to J.A.S.
Funders:
Funding AgencyGrant Number
Defense Advanced Research Projects Agency (DARPA)UNSPECIFIED
Merck and CompanyUNSPECIFIED
Searle Scholars ProgramUNSPECIFIED
NSFUNSPECIFIED
NIH Predoctoral FellowshipUNSPECIFIED
Issue or Number:19
PubMed Central ID:PMC328881
Record Number:CaltechAUTHORS:20160510-145810397
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160510-145810397
Official Citation:Jumi A. Shin, Richard H. Ebright, and Peter B. Dervan Orientation of the Lac repressor DNA binding domain in complex with the left lac operator half site characterized by affinity cleaving Nucl. Acids Res. (1991) 19 (19): 5233-5236 doi:10.1093/nar/19.19.5233
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ID Code:66953
Collection:CaltechAUTHORS
Deposited By: Victoria Brennan
Deposited On:17 May 2016 20:37
Last Modified:03 Oct 2019 10:01

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