Publications by authors named "Vladimir Mindel"
Article Synopsis
- This study focuses on how DNA-binding domains in transcription factors recognize specific sequence motifs in genomes, but in reality, they only bind to a small fraction of these motifs due to interactions with other transcription factors.
- The researchers developed a new method to test TF binding in yeast cells, allowing them to analyze thousands of designed sequences and measure how various transcription factors interacted with clusters of these motifs.
- The findings suggest that most TF binding can be explained by their independent interactions with individual motifs rather than by cooperative interactions between them, challenging previous ideas about how these factors work together in the genome.
Activation domains (ADs) within transcription factors (TFs) induce gene expression by recruiting coactivators such as the Mediator complex. Coactivators lack DNA binding domains (DBDs) and are assumed to passively follow their recruiting TFs. This is supported by direct AD-coactivator interactions seen in vitro but has not yet been tested in living cells.
View Article and Find Full Text PDFIntrinsically disordered regions (IDRs) are abundant in eukaryotic proteins, but their sequence-function relationship remains poorly understood. IDRs of transcription factors (TFs) can direct promoter selection and recruit coactivators, as shown for the budding yeast TF Msn2. To examine how IDRs encode both these functions, we compared genomic binding specificity, coactivator recruitment, and gene induction amongst a large set of designed Msn2-IDR mutants.
View Article and Find Full Text PDFWhite-rot fungi secrete a repertoire of high-redox potential oxidoreductases to efficiently decompose lignin. Of these enzymes, versatile peroxidases (VPs) are the most promiscuous biocatalysts. VPs are attractive enzymes for research and industrial use but their recombinant production is extremely challenging.
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