Using Protein-Fragment Complementation Assays (PCA) and Peptide Arrays to Study Telomeric Protein-Protein Interactions
Studying protein-protein interactions is critical to our understanding of signaling pathways. Telomere Interactome is assembled around telomeres and consists of proteins and factors from diverse pathways. Dissecting how this protein network contributes to telomere protection and length regulation requires the elucidation of the complex and dynamic interactions between the proteins within the interactome. Here, we focus on three assays, Bi-molecular Fluorescence Complementation (BiFC), Gaussia Luciferase Protein-fragment Complementation Assay (GLuc PCA), and OPAL peptide array, which have proven vital in our studies of telomere protein interaction networks.
Key wordsTelomere interactome Protein-protein interaction Telomere Protein fragment complementation (PCA) BiFC GLuc PCA Peptide array
We would like to acknowledge the support of NIGMS GM095599, CPRIT RP160462, the Welch Foundation Q-1673, and the C-BASS Shared Resource (with special thanks to Dr. Jun Xu) at the Dan L. Duncan Cancer Center (DLDCC) of Baylor College of Medicine (P30CA125123). This work was also supported by the National Basic Research Program (973 Program 2012CB911201), the National Natural Science Foundation of China (NSFC 91213302, 81330055, and 31371508), the Program of International S&T Cooperation (2014DFB30020), and the Science and Technology Planning Project of Guangdong Province (2015B020228002).