PMID: 9543002May 23, 1998Paper

Identification of indispensable residues for specific DNA-binding in the imperfect tandem repeats of c-Myb R2R3

Protein Engineering
M OdaH Nakamura

Abstract

The individual repeats, R2 and R3, of the minimum specific DNA-binding domain (R2R3) of c-Myb have very similar structures, with a helix-turn-helix variation motif, although their sequence identity in the tandem repeats is only 31%. From previous mutational and structural studies, the third helices in both repeats were shown to directly recognize the specific base sequence, PyAACG/TG. In order to elucidate the reason for the imperfection of the tandem repeats at amino acid positions other than the recognition helices, a series of R2R3 mutants was generated by swapping the helices and the N-terminus in R2 to those in R3. Consequently, the sequence composing the first helix of R2 was found to be essential for specific DNA-binding, in addition to the third recognition helix of R2. Further mutational studies revealed that the only indispensable residues in the first helix are Val103 and Val1O7, which are involved in the hydrophobic core of R2. These residues do not directly interact with the DNA, but they contribute to the correct formation of helix 1 and the characteristic packing of R2, which is slightly different from that of R3, and are required for specific base recognition through strong cooperativity with R3.

Citations

Jul 31, 2013·Archives of Biochemistry and Biophysics·Satomi InabaMasayuki Oda
Mar 30, 2013·Computational Biology and Chemistry·R M RamosI S Moreira
Jul 11, 2000·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·M Oda, H Nakamura
Dec 17, 2009·BMC Developmental Biology·Gary C HorvathW Stephen Kistler
Oct 2, 2002·The Journal of Biological Chemistry·Lisette MohrmannC Peter Verrijzer
May 13, 2021·Biophysics and Physicobiology·Maki Kawasaki, Masayuki Oda

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