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The ancillary N-terminal region of the yeast AP-1 transcription factor Yap8 contributes to its DNA binding specificity.

Journal article
Authors Ewa Maciaszczyk-Dziubinska
Anna Reymer
Nallani Vijay Kumar
Wojciech Białek
Katarzyna Mizio
Markus J. Tamás
Robert Wysocki
Published in Nucleic acids research
Volume 48
Issue 10
Pages 5426-5441
ISSN 1362-4962
Publication year 2020
Published at Department of Chemistry and Molecular Biology
Pages 5426-5441
Language en
Links dx.doi.org/10.1093/nar/gkaa316
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Microbiology, Biochemistry and Molecular Biology, Physical Chemistry

Abstract

Activator protein 1 (AP-1) is one of the largest families of basic leucine zipper (bZIP) transcription factors in eukaryotic cells. How AP-1 proteins achieve target DNA binding specificity remains elusive. In Saccharomyces cerevisiae, the AP-1-like protein (Yap) family comprises eight members (Yap1 to Yap8) that display distinct genomic target sites despite high sequence homology of their DNA binding bZIP domains. In contrast to the other members of the Yap family, which preferentially bind to short (7-8 bp) DNA motifs, Yap8 binds to an unusually long DNA motif (13 bp). It has been unclear what determines this unique specificity of Yap8. In this work, we use molecular and biochemical analyses combined with computer-based structural design and molecular dynamics simulations of Yap8-DNA interactions to better understand the structural basis of DNA binding specificity determinants. We identify specific residues in the N-terminal tail preceding the basic region, which define stable association of Yap8 with its target promoter. We propose that the N-terminal tail directly interacts with DNA and stabilizes Yap8 binding to the 13 bp motif. Thus, beside the core basic region, the adjacent N-terminal region contributes to alternative DNA binding selectivity within the AP-1 family.

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