Joseph B. Bridgers

ORCID: 0000-0002-0585-4131
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About
Contact & Profiles
Research Areas
  • Genomics and Chromatin Dynamics
  • Peptidase Inhibition and Analysis
  • Cancer Mechanisms and Therapy
  • Ubiquitin and proteasome pathways
  • Protein Degradation and Inhibitors
  • Epigenetics and DNA Methylation
  • RNA modifications and cancer
  • Plant Molecular Biology Research
  • RNA and protein synthesis mechanisms
  • Cancer-related gene regulation
  • Plant Virus Research Studies
  • Signaling Pathways in Disease
  • Histone Deacetylase Inhibitors Research
  • Fungal and yeast genetics research
  • Gene Regulatory Network Analysis
  • Pharmacological Receptor Mechanisms and Effects
  • Molecular Biology Techniques and Applications
  • ATP Synthase and ATPases Research
  • Mitochondrial Function and Pathology
  • Mechanisms of cancer metastasis
  • RNA Research and Splicing

Harvard University
2025

University of North Carolina at Chapel Hill
2015-2019

UNC Lineberger Comprehensive Cancer Center
2017

Indiana University School of Medicine
2017

Metabolic signaling to chromatin often underlies how adaptive transcriptional responses are controlled. While intermediary metabolites serve as co-factors for histone-modifying enzymes during metabolic flux, these modifications contribute is poorly understood. Here, we utilize the highly synchronized yeast cycle (YMC) and find that fatty acid β-oxidation genes periodically expressed coincident with byproduct histone crotonylation. Specifically, found H3K9 crotonylation peaks when acetylation...

10.1016/j.molcel.2019.09.029 article EN publisher-specific-oa Molecular Cell 2019-10-30

The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity bind histone lysine acetylation. Here, we show that domain Taf14, member key transcriptional and chromatin-modifying complexes yeast, is selective reader H3 Lys9 acetylation (H3K9ac). Structural analysis reveals acetylated sandwiched an aromatic cage formed by F62 W81. Disruption this binding cells impairs gene transcription DNA damage response. Our findings establish highly...

10.1101/gad.269977.115 article EN Genes & Development 2015-09-01

Histone posttranslational modifications (PTMs) function to regulate chromatin structure and in part through the recruitment of effector proteins that harbor specialized "reader" domains. Despite efforts elucidate reader domain–PTM interactions, influence neighboring PTMs target specificity many domains is still unclear. The aim this study was use a high-throughput histone peptide microarray platform interrogate 83 known putative from chromo Tudor domain families identify their interactions...

10.1186/s13072-017-0117-5 article EN cc-by Epigenetics & Chromatin 2017-03-14

Mitochondrial gene expression is essential for oxidative phosphorylation. Mitochondrial-encoded mRNAs are translated by dedicated mitochondrial ribosomes (mitoribosomes), whose regulation remains elusive. In the baker's yeast Saccharomyces cerevisiae , nuclear-encoded translational activators (TAs) facilitate transcript-specific translation a yet unknown mechanism. Here, we investigated function of TAs containing RNA-binding pentatricopeptide repeats (PPRs) using selective mitoribosome...

10.1101/2025.01.26.634913 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2025-01-26

Mitochondrial gene expression needs to be balanced with cytosolic translation produce oxidative phosphorylation complexes. In yeast, translational feedback loops involving lowly expressed proteins called activators help achieve this balance. Synthesis of cytochrome b (Cytb or COB), a core subunit complex III in the respiratory chain, is controlled by three and assembly factor Cbp3-Cbp6. However, molecular interface between COB loop yet unknown. Here, using protein-proximity mapping combined...

10.1101/2025.01.30.635641 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2025-01-31

Yaf9 is an integral part of the NuA4 acetyltransferase and SWR1 chromatin remodeling complexes. Here, we show that associates with acetylated histone H3 high preference for H3K27ac. The crystal structure YEATS domain bound to H3K27ac peptide reveals sequence C-terminal K27ac stabilizes complex. side chain inserts between two aromatic residues, mutation which abrogates interaction in vitro leads vivo phenotypes similar YAF9 deletion, including loss SWR1-dependent incorporation variant H2A.Z....

10.1093/nar/gkx1151 article EN cc-by-nc Nucleic Acids Research 2017-10-31

The plant homeodomain (PHD) finger is found in many chromatin-associated proteins and functions to recruit effector chromatin through its ability bind both methylated unmethylated histone residues. Here, we show that the dual PHD fingers of Rco1, a member Rpd3S deacetylase complex recruited transcribing genes, operate combinatorial manner targeting H3 chromatin. Although mutations either first or second allow for formation, assembled complexes from these mutants cannot recognize nucleosomes...

10.1074/jbc.m116.720193 article EN cc-by Journal of Biological Chemistry 2016-05-17
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