Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba, Japan.
Published: March 2013
AI Article Synopsis
Article Abstract
Terminal deoxynucleotidyltransferase (TdT), which template-independently synthesizes DNA during V(D)J recombination in lymphoid cells, is ubiquitylated by a BPOZ-2/Cul3 complex, as the ubiquitin ligase, and then degraded by the 26 S proteasome. We show here that TdT is ubiquitylated by the Cul3-based ubiquitylation system in vitro. Because TdT could also be ubiquitylated in the absence of Cul/BPOZ-2, we determined that it could also be directly ubiquitylated by the E2 proteins UbcH5a/b/c and UbcH6, E3-independently. Furthermore, the ubiquitylated TdT inhibited its nucleotidyltransferase activity.
The Mucin1 (MUC1) protein, involved in cytoprotective and signaling pathways, is abnormally elevated in various cancers, making it a key cancer indicator. Exosomes, which reflect the status of their originating cells, offer potential for cancer diagnosis. Thus, developing a method to detect MUC1-positive exosomes is crucial for the early diagnosis of certain cancers.
The excessive use of cobalt in various chemical industries and arbitrary discharge of industrial wastewater have led to increased cobalt pollution in soil and water resources, increasing the risk of human exposure to high concentrations of cobalt and necessitating an urgent need for on-site monitoring platform for cobalt pollution. In this study, the terminal deoxynucleotidyl transferase (TdT)-CRISPR platform has been developed. In this platform, cobalt as a cofactor of TdT, can significantly improve the tailing efficiency of TdT-mediated extension.
This study aimed to investigate the effects of Miao medicinal RS3-resistant starch on behavioral performance and substantia nigra neuron apoptosis-related indicators in a rat model of Parkinson's disease (PD). Among the experimental groups, except for the control group, we induced PD rat models by subcutaneous injection of rotenone in the neck and back. After model induction, a 28-day drug intervention was conducted.
Terminal deoxynucleotidyl transferase (TdT) is a unique DNA polymerase capable of template-independent extension of DNA. TdT's DNA synthesis ability has found utility in DNA recording, DNA data storage, oligonucleotide synthesis, and nucleic acid labeling, but TdT's intrinsic nucleotide biases limit its versatility in such applications. Here, we describe a multiplexed assay for profiling and engineering the bias and overall activity of TdT variants with high throughput.
