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EMBO J. 1992 Nov;11(11):4103-9.

Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif.

Author information

1
Marie Curie Research Institute, Oxted, Surrey, UK.

Abstract

While all basic region/helix-loop-helix (bHLH) proteins bind the consensus CANNTG motif, other factors must be involved in determining regulatory specificity. In this report we show that bases outside this core 6 bp are involved in determining the specificity of binding. Thus, binding of the yeast bHLH protein PHO4, but not CPF-1, is inhibited by the presence of a T residue immediately 5' to their common CACGTG recognition sequence. PHO4 binding specificity is altered by mutation at any of three different positions in the basic region, including a single Glu to Asp substitution. The significance of these data for DNA-binding and transcription regulation by the bHLH family of transcription factors is discussed.

PMID:
1327757
PMCID:
PMC556920
[Indexed for MEDLINE]
Free PMC Article

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