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Nucleic Acids Research, 1991, Vol. 19, No. 20 5645-5651
© 1991

MOLECULAR BIOLOGY

The four human muscle regulatory helix-loop-helix proteins Myf3-Myf6 exhibit similar hetero-dimerizartion and DNA binding properties

Thomas Braun and Hans Henning Arnold*

Department of Toxicology, Medical School, University of Hamburg Grindelallee 117, 2000 Hamburg 13, FRG

*To whom correspondence should be addressed

Received July 8, 1991. Accepted September 20, 1991.

The muscle regulatory proteins Myf3, Myf4, Myf5, and Myf6 share a highly conserved DNA binding and dimerization domain consisting of a cluster of basic amino acids and a potential helix-loop-helix structure. Here we demonstrate that the four human usclespecific HLH proteins have similar DNA binding and dimerization properties. The members of this family form protein complexes of comparable stability with the ubiquitously expressed HLH proteins E12, E2-2, and E2-5 and bind to the conserved DNA sequence CANNTG designated as E-box with similar efficiency in vitro. The binding affinities of the various complexes are greatly influenced by the variable internal and flanking nucleotides of the consensus motif. Combinations of Myf proteins with one another and with lyl-1, an HLH protein from human T cells, do not bind to DNA in vitro. Our results suggest that combinatorial associations of the various tissuespecific and more widely expressed HLH factors do not result in differential recognition of DNA sequences by Myf proteins.


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