The tryptophan cluster: a hypothetical structure of the DNA-binding domain of the myb protooncogene product

In the DNA-binding domain of the c-myb protooncogene product (c-Myb) which consists of three repeats of 51-52 amino acids, there are 3 perfectly conserved tryptophans in each repeat. Site-directed mutagenesis of these tryptophans showed that any single or multiple mutations of tryptophan to hydrophi...

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Veröffentlicht in:The Journal of biological chemistry 1990-11, Vol.265 (32), p.19990-19995
Hauptverfasser: Kanei-Ishii, C, Sarai, A, Sawazaki, T, Nakagoshi, H, He, D N, Ogata, K, Nishimura, Y, Ishii, S
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Sprache:eng
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Zusammenfassung:In the DNA-binding domain of the c-myb protooncogene product (c-Myb) which consists of three repeats of 51-52 amino acids, there are 3 perfectly conserved tryptophans in each repeat. Site-directed mutagenesis of these tryptophans showed that any single or multiple mutations of tryptophan to hydrophilic residues or alanine abolished or greatly reduced the sequence-specific DNA-binding activity, but mutations to hydrophobic amino acids retained considerable activity. Raman spectroscopic study showed that these tryptophans were buried in the protein core. These 3 tryptophans are proposed to form a cluster in the hydrophobic core in each repeat. This hypothetical structure is referred to as the “tryptophan cluster,” and it may represent a characteristic property of a group of DNA-binding proteins including the myb- and ets-related proteins.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)45472-X