DNA binding site of the yeast heteromeric Ino2p/Ino4p basic helix‐loop‐helix transcription factor: structural requirements as defined by saturation mutagenesis

FEBS Letters

Schüller, Hans-Joachim¹  Ebbert, Ronald¹  Richter, Karin¹  Hoffmann, Brigitte¹  Schweizer, Eckhart¹ 

[1] Institut für Mikrobiologie, Biochemie and Genetik, Lehrstuhl Biochemie, Universität Erlangen/Nürnberg, Staudtstr. 5, D-91058 Erlangen, Germany

关键词: bHLH transcription factor;    Phospholipid biosynthesis;    Saturation mutagenesis;    UAS element;    Saccharomyces cerevisiae;    bHLH;    basic helix-loop-helix;    CDE;    centromere DNA element;    ICRE;    inositol/choline-responsive element;    UAS;    upstream activation site;   

DOI  :  10.1016/0014-5793(95)00818-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The inositol/choline-responsive element (ICRE) is an 11 bp cis-activating sequence motif with central importance for the regulated expression of phospholipid biosynthetic genes in the yeast Saccharomyces cerevisiae. The ICRE containing the CANNTG core binding sequence (E-box) of basic helix-loop-helix (bHLH) regulatory proteins is recognized by the heteromeric bHLH transcription factor Ino2p/Ino4p. In this study, we define the Ino2p/Ino4p consensus binding sequence (5′-WYTTCAYR-TGS-3′) based on the characterization of all possible single nucleotide substitutions. Interestingly, this analysis also identified a single functional deviation (CACATTC) from the CANNTG core recognition element of bHLH proteins. The DNA binding specificities of different yeast bHLH proteins may now be explained by distinct nucleotide preferences especially at two positions immediately preceding the CANNTG core motif.

【 授权许可】

Unknown