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Dylan J. Taatjes

Dylan J. Taatjes

· Assistant Professor (Biochemistry)

University of Colorado Boulder · Molecular, Cellular & Developmental Biology

Active 1970–2025

h-index52
Citations13.6k
Papers13247 last 5y
Funding$13.4M1 active

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Professor Dylan J. Taatjes is a researcher at the University of Colorado Boulder, leading the Taatjes Lab which focuses on understanding the molecular mechanisms that control human gene expression. His work investigates how transcription and signaling pathways are altered during development and disease, with particular emphasis on sequence-specific, DNA-binding transcription factors and the Pre-Initiation Complex (PIC). The PIC, which includes components such as Mediator, RNA polymerase II, and various general transcription factors, plays a crucial role in regulating the activity of RNA polymerase II, the enzyme responsible for transcribing all protein-coding genes and most non-coding RNAs in the human genome. Professor Taatjes's research aims to elucidate how complexes like Mediator, TFIID, and TFIIH regulate transcription initiation and post-initiation processes, utilizing a variety of experimental techniques including biochemical, biophysical, molecular, cell biology, metabolomics, proteomics, and transcriptomics. His work contributes to a deeper understanding of gene regulation mechanisms in human development and disease.

Research topics

  • Biology
  • Cell biology
  • Computational biology
  • Computer Science
  • Genetics
  • Molecular biology
  • Biochemistry
  • Medicine
  • Internal medicine

Selected publications

  • An atlas of substrate specificities for the human serine/threonine kinome

    Nature · 2023 · 685 citations

    . Here we used synthetic peptide libraries to profile the substrate sequence specificity of 303 Ser/Thr kinases, comprising more than 84% of those predicted to be active in humans. Viewed in its entirety, the substrate specificity of the kinome was substantially more diverse than expected and was driven extensively by negative selectivity. We used our kinome-wide dataset to computationally annotate and identify the kinases capable of phosphorylating every reported phosphorylation site in the hum…

  • Partitioning of cancer therapeutics in nuclear condensates

    Science · 2020 · 517 citations

    The nucleus contains diverse phase-separated condensates that compartmentalize and concentrate biomolecules with distinct physicochemical properties. Here, we investigated whether condensates concentrate small-molecule cancer therapeutics such that their pharmacodynamic properties are altered. We found that antineoplastic drugs become concentrated in specific protein condensates in vitro and that this occurs through physicochemical properties independent of the drug target. This behavior was als…

  • Structure and mechanism of the RNA polymerase II transcription machinery

    Genes & Development · 2020 · 295 citations

    Senior authorCorresponding

    RNA polymerase II (Pol II) transcribes all protein-coding genes and many noncoding RNAs in eukaryotic genomes. Although Pol II is a complex, 12-subunit enzyme, it lacks the ability to initiate transcription and cannot consistently transcribe through long DNA sequences. To execute these essential functions, an array of proteins and protein complexes interact with Pol II to regulate its activity. In this review, we detail the structure and mechanism of over a dozen factors that govern Pol II initi…

  • Selective inhibition of CDK7 reveals high-confidence targets and new models for TFIIH function in transcription

    Genes & Development · 2020 · 85 citations

    Senior authorCorresponding

    CDK7 associates with the 10-subunit TFIIH complex and regulates transcription by phosphorylating the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Few additional CDK7 substrates are known. Here, using the covalent inhibitor SY-351 and quantitative phosphoproteomics, we identified CDK7 kinase substrates in human cells. Among hundreds of high-confidence targets, the vast majority are unique to CDK7 (i.e., distinct from other transcription-associated kinases), with a subset that suggest no…

  • Interaction between MED12 and ΔNp63 activates basal identity in pancreatic ductal adenocarcinoma

    Nature Genetics · 2024-06-17 · 14 citations

    articleOpen access

Recent grants

Frequent coauthors

  • Robin D. Dowell

    University of Colorado Anschutz Medical Campus

    51 shared
  • Cecilia B. Levandowski

    University of Colorado Boulder

    46 shared
  • Benjamin Erickson

    University of Colorado Boulder

    45 shared
  • David L. Bentley

    45 shared
  • Merve Çakır

    Duke University

    38 shared
  • Andrew M. Waters

    University of Cincinnati

    38 shared
  • Shannon J. McCall

    Duke University Health System

    38 shared
  • Alejandro Barrera

    Duke University

    38 shared

Labs

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