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Updated: May 31, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Competitive inhibition of transcription factors by small interfering peptides
Pil Joon Seo1, Shin-Young Hong, Sang-Gyu Kim
1Department of Chemistry, Seoul National University, Seoul 151-742, Korea.
Abstract:
Combinatorial assortment by dynamic dimer formation diversifies gene transcriptional specificities of transcription factors. A similar but biochemically distinct mechanism is competitive inhibition in which small proteins act as negative regulators by competitively forming nonfunctional heterodimers with specific transcription factors. The most extensively studied is the negative regulation of auxin response factors by AUXIN/INDOLE-3-ACETIC ACID repressors. Similarly, Arabidopsis thaliana (Arabidopsis) little zipper and mini finger proteins act as competitive inhibitors of target transcription factors. Competitive inhibitors are also generated by alternative splicing and controlled proteolytic processing. Because they provide a way of attenuating transcription factors we propose to call them small interfering peptides (siPEPs). The siPEP-mediated strategy could be applied to deactivate specific transcription factors in crop plants.
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