Specific binding between Arabidopsis thaliana phytochrome-interacting factor 3 (AtPIF3) bHLH and G-box originated prior to embryophyte emergence.

ABSTRACT: The basic helix-loop-helix (bHLH) domain via critical amino acid residues on basic region binding to E-box (5'-CANNTG-3') is known in embryophyte. However, the dictated E-box types selection by bHLH dimers and the significant impact of these critical amino acid residues along embryophyte evolution remain unclear. The Arabidopsis thaliana PIF3-bHLH (AtPIF3-bHLH) recombinant protein and a series of AtPIF3-bHLH mutants were synthesized and analyzed. The reduced DNA binding ability and affinity of AtPIF3-bHLH point-mutation proteins, observed via fluorescence-based electrophoretic mobility shift assay (fEMSA) and isothermal titration calorimetry (ITC), suggest the critical role of these DNA-recognition sites in maintaining the AtPIF3-bHLH-DNA interaction. The purifying selection signals and th

SUBMITTER: Hsin KT 

PROVIDER: S-EPMC11552376 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature