التفاصيل البيبلوغرافية
| العنوان: |
Specific binding between Arabidopsis thaliana phytochrome-interacting factor 3 (AtPIF3) bHLH and G-box originated prior to embryophyte emergence. |
| المؤلفون: |
Hsin, Kuan-Ting, Lee, Yu-Hsuan, Lin, Kai-Chun, Chen, Wei, Cheng, Yi-Sheng |
| المصدر: |
BMC Plant Biology; 11/11/2024, Vol. 24 Issue 1, p1-17, 17p |
| مصطلحات موضوعية: |
AMINO acid residues, ISOTHERMAL titration calorimetry, DNA-protein interactions, RECOMBINANT proteins, ARABIDOPSIS thaliana |
| مستخلص: |
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 the DNA-recognition-site conservation at the species level suggest the invariant roles of these sites throughout embryophyte evolution. The G-box outcompeted other types of E-box for binding in our competitive fEMSAs. The dynamic hydrogen bond formed between AtPIF3-bHLH and the G-box core indicates flexible identification of the core region. These features highlight a fast fixation of the bHLH-G-box recognition mechanism through embryophyte evolution and serve as a blueprint for studying DNA recognition determinants of other TF families. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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