The interaction between the purine motif triplex and the triplex DNA-binding domain of Saccharomyces cerevisiae Stm1 protein.
Saccharomyces cerevisiae Stm1 protein (273 amino acids) is a purine motif triplex DNA-binding protein. We have previously found that Stm(1-113) (amino acids 1-113) is the minimal domain to specifically bind with the purine motif triplex. Here, to reveal the triplex recognition mechanism of Stm(1-113), we have examined the interaction between Stm(1-113) and each of the purine motif triplexes with various lengths and base sequences. As the length of the target triplex was increased, the binding affinity of Stm(1-113) to the target triplex was increased. Stm(1-113) had the ability to bind to the purine motif triplexes with various base sequences. We conclude that Stm(1-113) may recognize the shape of the triplex rather than the base sequence of the triplex.
Katayama
Takuma
T
Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan.
Torigoe
Hidetaka
H
D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D024202:Electrophoretic Mobility Shift Assay; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011687:Purines / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
D004268:DNA-Binding Proteins; D011687:Purines; D029701:Saccharomyces cerevisiae Proteins; C528347:Stm1 protein, S cerevisiae; C051802:triplex DNA; D004247:DNA