A5072370975- RNA Research and Splicing
- Protein Structure and Dynamics
- Endoplasmic Reticulum Stress and Disease
- Heat shock proteins research
- RNA and protein synthesis mechanisms
- Advancements in Semiconductor Devices and Circuit Design
- RNA modifications and cancer
- Semiconductor materials and devices
- Molecular Biology Techniques and Applications
- Advanced Electron Microscopy Techniques and Applications
Radboud University Nijmegen
2022-2024
Oncode Institute
2024
Radboud Institute for Molecular Life Sciences
2022-2023
Radboud University Medical Center
2022-2023
Small heat shock proteins (sHSPs) are essential ATP-independent chaperones that protect the cellular proteome. These assemble into polydisperse oligomeric structures, composition of which dramatically affects their chaperone activity. The biomolecular consequences variations in sHSP ratios, especially inside living cells, remain elusive. Here, we study altering relative expression levels HspB2 and HspB3 HEK293T cells. partners a hetero-oligomeric complex, genetic mutations abolish mutual...
SUMMARY Poly(A)-tails are crucial for mRNA translation and degradation, but the exact relationship between tail length kinetics remains unclear. Here we employ a small library of identical mRNAs that differ only in their poly(A)-tail to examine behavior human embryonic kidney cells. We find strongly correlates with degradation rates, is decoupled from translation. Interestingly, an optimal ∼100 nucleotides displays highest rate, which average endogenous measured by nanopore sequencing....
Quantifying the number of proteins that interact with mRNAs, in particular poly(A) tails is crucial for understanding gene regulation. Biochemical assays offer significant advantages this purpose. Here, we present a protocol synthesizing mRNAs accurate, length-specific through PCR-based approach. We also describe steps an vitro (i.e., cell-free) approach visualizing sequential binding Cytoplasmic Poly(A)-Binding Proteins (PABPCs) to these tails. detail quality control throughout procedure....
Summary Small heat shock proteins (sHSPs) are essential ATP-independent chaperones that protect the cellular proteome during stress. These assemble into polydisperse oligomeric structures, composition of which dramatically affects their chaperone activity. The biomolecular consequences variations in sHSP ratios, especially inside living cells, remain elusive. Here, we study altering relative expression levels HspB2 and HspB3. partners a hetero-oligomeric complex, genetic mutations abolish...