Curated collection of yeast transcription factor DNA binding specificity data reveals novel structural and gene regulatory insights.

Published

Journal Article

Transcription factors (TFs) play a central role in regulating gene expression by interacting with cis-regulatory DNA elements associated with their target genes. Recent surveys have examined the DNA binding specificities of most Saccharomyces cerevisiae TFs, but a comprehensive evaluation of their data has been lacking.We analyzed in vitro and in vivo TF-DNA binding data reported in previous large-scale studies to generate a comprehensive, curated resource of DNA binding specificity data for all characterized S. cerevisiae TFs. Our collection comprises DNA binding site motifs and comprehensive in vitro DNA binding specificity data for all possible 8-bp sequences. Investigation of the DNA binding specificities within the basic leucine zipper (bZIP) and VHT1 regulator (VHR) TF families revealed unexpected plasticity in TF-DNA recognition: intriguingly, the VHR TFs, newly characterized by protein binding microarrays in this study, recognize bZIP-like DNA motifs, while the bZIP TF Hac1 recognizes a motif highly similar to the canonical E-box motif of basic helix-loop-helix (bHLH) TFs. We identified several TFs with distinct primary and secondary motifs, which might be associated with different regulatory functions. Finally, integrated analysis of in vivo TF binding data with protein binding microarray data lends further support for indirect DNA binding in vivo by sequence-specific TFs.The comprehensive data in this curated collection allow for more accurate analyses of regulatory TF-DNA interactions, in-depth structural studies of TF-DNA specificity determinants, and future experimental investigations of the TFs' predicted target genes and regulatory roles.

Full Text

Duke Authors

Cited Authors

  • Gordân, R; Murphy, KF; McCord, RP; Zhu, C; Vedenko, A; Bulyk, ML

Published Date

  • December 21, 2011

Published In

Volume / Issue

  • 12 / 12

Start / End Page

  • R125 -

PubMed ID

  • 22189060

Pubmed Central ID

  • 22189060

Electronic International Standard Serial Number (EISSN)

  • 1474-760X

International Standard Serial Number (ISSN)

  • 1474-7596

Digital Object Identifier (DOI)

  • 10.1186/gb-2011-12-12-r125

Language

  • eng