Oxidative stress and damage is considered to be a significant causative factor in aging and neurodegenerative diseases. Concurrent with the clinical phenotypes associated with these diseases is mitochondrial dysfunction in the form of biochemical malfunctions that create or potentiate reactive oxygen species (ROS) production. Dihydrolipoamide dehydrogenase (DLD) is a mitochondrial multifunctional enzyme with a homodimeric structure, resolved as two monomers bridged by an interface domain. In its dimeric form, DLD plays a critical role in energy metabolism and has been suggested to have a destructive role as a generator of ROS in its monomeric form. The latter activity has been confirmed in prior studies in both mouse and yeast models. Decreased superoxide activity has been measured in DLD knockout (‐/‐) mice vs. WT mice (Starkov et al., 2004) and higher diaphorase activity with increased hydrogen peroxide levels (Vaubel et al., 2011) has been shown in DLD mutants expressed in yeast systems. Our lab using virtual screening and computational docking has designed a small molecule library containing 40 synthetic compounds that putatively bind to a pocket within the interface domain of DLD with the aim of stabilizing the dimer. Primary screening of the compound library using the diaphorase assay is in progress. Validation of hits will be performed using Differential Scanning Fluorimetry (DSF), X‐ray crystallography and other techniques including in‐vivo analyses. We hope that these studies will enhance our understanding of the physiological role of diaphorase activity and facilitate the development of therapeutics for pathologies in which diaphorase activity has a suggested damaging function.
A Classification Model for
BRCA2
DNA Binding Domain Missense Variants Based on Homology-Directed Repair Activity
Nephrolithiasis is a major public health problem with a complex and varied etiology. Most stones are composed of calcium oxalate (CaOx), with dietary excess a risk factor. Because of complexity of mammalian system, the details of stone formation remain to be understood. Here we have developed a nephrolithiasis model using the genetic model Drosophila melanogaster, which has a simple, transparent kidney tubule. Drosophilia reliably develops CaOx stones upon dietary oxalate supplementation, and the nucleation and growth of microliths can be viewed in real time. The Slc26 anion transporter dPrestin (Slc26a5/6) is strongly expressed in Drosophilia kidney, and biophysical analysis shows that it is a potent oxalate transporter. When dPrestin is knocked down by RNAi in fly kidney, formation of microliths is reduced, identifying dPrestin as a key player in oxalate excretion. CaOx stone formation is an ancient conserved process across >400 My of divergent evolution (fly and human), and from this study we can conclude that the fly is a good genetic model of nephrolithiasis.
Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1
Tyr142, the C-terminal amino acid of histone variant H2A.X is phosphorylated by WSTF (Williams-Beuren syndrome transcription factor), a component of the WICH complex (WSTF-ISWI chromatin-remodeling complex), under basal conditions in the cell. In response to DNA double-strand breaks (DSBs), H2A.X is instantaneously phosphorylated at Ser139 by the kinases ATM and ATR and is progressively dephosphorylated at Tyr142 by the Eya1 and Eya3 tyrosine phosphatases, resulting in a temporal switch from a postulated diphosphorylated (pSer139, pTyr142) to monophosphorylated (pSer139) H2A.X state. How mediator proteins interpret these two signals remains a question of fundamental interest. We provide structural, biochemical, and cellular evidence that Microcephalin (MCPH1), an early DNA damage response protein, can read both modifications via its tandem BRCA1 C-terminal (BRCT) domains, thereby emerging as a versatile sensor of H2A.X phosphorylation marks. We show that MCPH1 recruitment to sites of DNA damage is linked to both states of H2A.X.
Heparin-Degrading Sulfatases in Hepatocellular Carcinoma: Roles in Pathogenesis and Therapy Targets