A5037931256- RNA modifications and cancer
- RNA and protein synthesis mechanisms
- RNA Research and Splicing
- Genomics and Chromatin Dynamics
- Nuclear Structure and Function
- Heat shock proteins research
- Fungal and yeast genetics research
- Signaling Pathways in Disease
- Cancer-related gene regulation
- Fermentation and Sensory Analysis
- 14-3-3 protein interactions
- RNA regulation and disease
- Cellular Mechanics and Interactions
- Biochemical and Molecular Research
- Peptidase Inhibition and Analysis
- Fungal Biology and Applications
- FOXO transcription factor regulation
- Genetics, Aging, and Longevity in Model Organisms
- Viral Infections and Immunology Research
Southwestern Medical Center
2022-2024
The University of Texas Southwestern Medical Center
2003-2024
Dallas County
2022
ETH Zurich
2007-2015
University of California, Berkeley
2004-2009
Harvard University
2001-2003
Massachusetts General Hospital
2001-2003
To understand the role of chromatin-remodeling activities in transcription, it is necessary to how they interact with transcriptional activators vivo regulate different steps transcription. Human heat shock factor 1 (HSF1) stimulates both initiation and elongation. We replaced mouse HSF1 fibroblasts wild-type mutant human constructs characterized regulation an endogenous hsp70 gene. A mutation that diminished led twofold reductions mRNA induction recruitment a SWI/SNF remodeling complex. In...
Chromatin remodeling complexes such as SWI/SNF use the energy of ATP hydrolysis to remodel nucleosomal DNA and increase transcription templates. Human heat shock factor one (hHSF1) is a tightly regulated activator that stimulates transcriptional initiation elongation using different portions its activation domains. Here we demonstrate hHSF1 associates with BRG1, ATPase subunit human (hSWI/SNF) at endogenous protein concentrations. We also show domains recruit hSWI/SNF chromatin template in...
DEAD-box ATPases play crucial roles in guiding rRNA restructuring events during the biogenesis of large (60S) ribosomal subunits, but their precise molecular functions are currently unknown. In this study, we present cryo-EM reconstructions nucleolar pre-60S intermediates that reveal an unexpected, alternate secondary structure within nascent peptidyl-transferase-center (PTC). Our analysis three sequential reveals ATPase Dbp10/DDX54 remodels base pairing and enables formation junction...
The DExD/H-box RNA-dependent ATPase Dbp5 plays an essential role in the nuclear export of mRNA. localizes to pore complex, where its activity is stimulated by Gle1 and coactivator inositol hexakisphosphate. Here, we present crystal structure C-terminal domain Dbp5, refined 1.8 A. reveals a RecA-like fold that contains two defining characteristics not other structurally characterized proteins: alpha-helix loop connecting beta5 alpha4, both which are composed conserved unique elements primary...
Biogenesis of the large ribosomal (60S) subunit involves assembly three rRNAs and 46 proteins, a process requiring approximately 70 ribosome biogenesis factors (RBFs) that bind release pre-60S at specific steps along pathway. The methyltransferase Spb1 K-loop GTPase Nog2 are essential RBFs engage rRNA A-loop during sequential in 60S maturation. methylates nucleotide G2922 catalytically deficient mutant strain (spb1D52A) has severe defect. However, function this modification is currently...
Abstract DEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited vitro catalytic activities described for these is at odds with their complex cellular roles, most notably driving large-scale remodeling steps during assembly ribonucleoproteins (RNPs). We describe cryo-EM structures 60S ribosomal biogenesis intermediates that reveal how context-specific unwinding by ATPase Spb4 results extensive, sequence-directed rRNA secondary structure. Multiple...
Abstract DEAD-box ATPases play crucial roles in guiding rRNA restructuring events during the biogenesis of large (60S) ribosomal subunits, but their precise molecular functions are currently unknown. In this study, we present cryo-EM reconstructions nucleolar pre-60S intermediates that reveal an unexpected, alternate secondary structure within nascent peptidyl-transferase-center (PTC). Our analysis three sequential reveals ATPase Dbp10/DDX54 remodels base pairing and enables formation...
Abstract Biogenesis of the large ribosomal (60S) subunit involves assembly three rRNAs and 46 proteins, a process requiring approximately 70 ribosome biogenesis factors (RBFs) that bind release pre-60S at specific steps along pathway. The methyltransferase Spb1 K-loop GTPase Nog2 are essential RBFs engage rRNA A-loop during sequential in 60S maturation. methylates nucleotide G2922 catalytically deficient mutant strain ( spb1 D52A ) has severe defect. However, function this modification is...