- CRISPR and Genetic Engineering
- Genetics, Aging, and Longevity in Model Organisms
- Cell death mechanisms and regulation
- DNA Repair Mechanisms
- Mitochondrial Function and Pathology
- Coenzyme Q10 studies and effects
- Genomics, phytochemicals, and oxidative stress
- Endoplasmic Reticulum Stress and Disease
- RNA Interference and Gene Delivery
- Hepatitis B Virus Studies
University of Colorado Boulder
2012-2016
Mitochondria are inherited maternally in most animals, but the mechanisms of selective paternal mitochondrial elimination (PME) unknown. While examining fertilization Caenorhabditis elegans, we observed that mitochondria rapidly lose their inner membrane integrity. CPS-6, a endonuclease G, serves as factor is critical for PME. We found CPS-6 relocates from intermembrane space to matrix after degrade DNA. It acts with maternal autophagy and proteasome machineries promote Loss cps-6 delays...
HBx is a multifunctional hepatitis B virus (HBV) protein that crucial for HBV infection and pathogenesis contributing cause of hepatocyte carcinogenesis. However, the host targets mechanisms action are poorly characterized. We show here expression in Caenorhabditis elegans induces both necrotic apoptotic cell death, mimicking an early event liver by HBV. Genetic biochemical analyses indicate interacts directly with B-cell lymphoma 2 (Bcl-2) homolog CED-9 (cell death abnormal) through Bcl-2...
Endonuclease G (EndoG) is a mitochondrial protein that released from mitochondria and relocated into the nucleus to promote chromosomal DNA fragmentation during apoptosis. Here, we show oxidative stress causes cell-death defects in C. elegans through an EndoG-mediated pathway. In response high reactive oxygen species (ROS) levels, homodimeric CPS-6—the homolog of EndoG—is dissociated monomers with diminished nuclease activity. Conversely, activity CPS-6 enhanced, its dimeric structure...
Endonuclease G (EndoG) is a mitochondrial protein that traverses to the nucleus and participates in chromosomal DNA degradation during apoptosis yeast, worms, flies, mammals. However, it remains unclear how EndoG binds digests DNA. Here we show Caenorhabditis elegans CPS-6, homolog of EndoG, homodimeric Mg2+-dependent nuclease, binding preferentially G-tract optimum low salt buffer at pH 7. The crystal structure CPS-6 was determined 1.8 Å resolution, revealing mixed αβ topology with two...