Structural properties of the DNA-bound form of a novel tandem repeat DNA-binding domain, STPR

Proteins
Shin SaitoKeiichi Kawano

Abstract

Fibroin-modulator-binding protein 1 (FMBP-1) is a predicted transcription factor of the silkworm fibroin gene. The DNA-binding domain of FMBP-1 consists of four almost perfect tandem repeats of 23 amino acids each (R1-R4), and is referred to as the score and three amino acid peptide repeat (STPR) domain. This characteristic domain is conserved in eukaryotes, but the DNA-binding mode is not known. In this study, the structural properties of the DNA-bound form of the STPR domain were characterized. The combined experiments indicated that the STPR domain bound to the DNA duplex with a 1:1 binding ratio. The specific DNA caused considerable changes in the thermal unfolding profile and the digestion pattern of the STPR domain. These data suggested that the domain adapts a quite rigid helix-rich structure in the DNA-bound state, even though it moves flexibly in the absence of DNA. Furthermore, mutual induced-fit conformational change was also observed in DNA. Finally, we determined the DNA-binding surface of the STPR third repeat (R3) by alanine scanning mutagenesis; a particular site, composed of hydrophobic and hydrophilic residues, was identified. Notably, the substitution of Arg-9 in R3 with alanine residue, which is located in t...Continue Reading

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Citations

Mar 24, 2009·Journal of Biochemistry·Shigeharu TakiyaKeiichi Kawano
Mar 5, 2016·Nucleic Acids Research·Li-Yan YuCong-Zhao Zhou
Mar 13, 2014·Journal of the American Chemical Society·Tomohisa SawadaMakoto Fujita

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