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Comparative Study | Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.

Determinants of DNA-binding specificity of ETS-domain transcription factors.

P Shore, A J Whitmarsh, R Bhaskaran, R J Davis, J P Waltho, A D Sharrocks
P Shore
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, United Kingdom.
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A J Whitmarsh
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, United Kingdom.
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R Bhaskaran
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, United Kingdom.
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R J Davis
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, United Kingdom.
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J P Waltho
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, United Kingdom.
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A D Sharrocks
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, United Kingdom.
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DOI: 10.1128/MCB.16.7.3338
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ABSTRACT

Several mechanisms are employed by members of transcription factor families to achieve sequence-specific DNA recognition. In this study, we have investigated how members of the ETS-domain transcription factor family achieve such specificity. We have used the ternary complex factor (TCF) subfamily as an example. ERK2 mitogen-activated protein kinase stimulates serum response factor-dependent and autonomous DNA binding by the TCFs Elk-1 and SAP-la. Phosphorylated Elk-1 and SAP-la exhibit specificities of DNA binding similar to those of their isolated ETS domains. The ETS domains of Elk-1 and SAP-la and SAP-2 exhibit related but distinct DNA-binding specificities. A single residue, D-69 (Elk-1) or V-68 (SAP-1), has been identified as the critical determinant for the differential binding specificities of Elk-1 and SAP-1a, and an additional residue, D-38 (Elk-1) or Q-37 (SAP-1), further modulates their DNA binding. Creation of mutations D38Q and D69V is sufficient to confer SAP-la DNA-binding specificity upon Elk-1 and thereby allow it to bind to a greater spectrum of sites. Molecular modelling indicates that these two residues (D-38 and D-69) are located away from the DNA-binding interface of Elk-1. Our data suggest a mechanism in which these residues modulate DNA binding by influencing the interaction of other residues with DNA.

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Determinants of DNA-binding specificity of ETS-domain transcription factors.
P Shore, A J Whitmarsh, R Bhaskaran, R J Davis, J P Waltho, A D Sharrocks
Molecular and Cellular Biology Jul 1996, 16 (7) 3338-3349; DOI: 10.1128/MCB.16.7.3338

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Determinants of DNA-binding specificity of ETS-domain transcription factors.
P Shore, A J Whitmarsh, R Bhaskaran, R J Davis, J P Waltho, A D Sharrocks
Molecular and Cellular Biology Jul 1996, 16 (7) 3338-3349; DOI: 10.1128/MCB.16.7.3338
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