Arginine (348) is a major determinant of the DNA binding specificity of transcription factor E12

Sieber, M. and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 1998. Arginine (348) is a major determinant of the DNA binding specificity of transcription factor E12. Biological Chemistry 379 (6) , pp. 731-735.

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Abstract

The basic helix-loop-helix proteins (BHLH) E12 and E47 bind to DNA in a cell-type specific fashion as heterodimers with transcription factors such as MyoD, Myf-5, MRF-4, myogenin, and MASH-1 and -2 which are critical regulators of cellular differentiation. We have measured the apparent dissociation constants (KD) of the complexes of E12 and several E12 mutants with various oligonucleotides. Glutamate (345) of E12, which is hydrogen bonded to a CpA dinucleotide, and arginine (348), a residue that does not directly interact with the nucleobases, are major determinants of the DNA binding specificity of E12. R(348) is in direct contact with both the phosphate backbone and the carboxylate of E(345), thereby locking the side chain conformation of E(345). In its locked conformation the glutamate residue interacts favourably only with E-box containing DNA, the natural target of BHLH-proteins, while repulsive interactions destabilise the complexes with all other DNA sequences.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry Cardiff Catalysis Institute (CCI)
Subjects:	Q Science > QD Chemistry
Publisher:	de Gruyter
ISSN:	1431-6730
Last Modified:	18 Oct 2022 13:50
URI:	https://orca.cardiff.ac.uk/id/eprint/15651

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