- RNA modifications and cancer
- RNA and protein synthesis mechanisms
- RNA Research and Splicing
- Photosynthetic Processes and Mechanisms
- Respiratory viral infections research
- Genomics and Chromatin Dynamics
- Enzyme Structure and Function
- Influenza Virus Research Studies
Vanderbilt University
2020-2023
mRNA in eukaryotic cells is packaged into highly compacted ribonucleoprotein particles (mRNPs) the nucleus and exported to cytoplasm for translation. mRNP packaging export require evolutionarily conserved transcription-export (TREX) complex. TREX facilitates loading of various RNA-binding proteins on through action its DDX39B subunit. SARNP (Tho1 [transcriptional defect Hpr1 by overexpression 1] yeast) shown interact with affect export. The molecular mechanism how recognizes functions...
The evolutionarily conserved TRanscript-EXport (TREX) complex plays central roles during mRNP (messenger ribonucleoprotein) maturation and export from the nucleus to cytoplasm. In yeast, TREX is composed of THO sub-complex (Tho2, Hpr1, Tex1, Mft1, Thp2), DEAD box ATPase Sub2, Yra1. Here we present a 3.7 Å cryo-EM structure yeast THO•Sub2 complex. reveals intimate assembly revolving around its largest subunit Tho2. stabilizes semi-open conformation Sub2 via interactions with We show that...
Significance Gene transcription from DNA to RNA by Polymerase II (Pol II) is regulated a group of cyclin-dependent kinases (CDKs). In order coordinate the molecular events during transcription, CDKs enzymatically modify Pol II. Here, we determined crystal structure an important CDK involved in regulation, yeast C-terminal domain kinase-1 (CTDK-1) complex, describe its architecture atomic detail. Importantly, CTDK-1 reveals mechanism for activation enzyme. addition, show that interacts with...
Abstract The evolutionarily conserved TREX complex plays central roles during mRNP (messenger ribonucleoprotein) maturation and export from the nucleus to cytoplasm. In yeast, is composed of THO sub-complex (Tho2, Hpr1, Tex1, Mft1, Thp2), DEAD box ATPase Sub2, Yra1. Here we present a 3.7 Å cryo-EM structure yeast THO•Sub2 complex. reveals intimate assembly revolving around its largest subunit Tho2. stabilizes semi-open conformation Sub2 via interactions with We show that interacts SR-like...