Uncovering Protein Complexes and Assemblies: Stories of Dynamic Virus-Host Interactions and Specific Synapse Characterization |
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| Air date: | Friday, November 07, 2008, 10:00:00 AM |
| Category: | Proteomics |
| Description: | Isolation of protein complexes, if performed appropriately, can provide an invaluable shortcut to uncovering protein interactions and to gaining clues towards their biological functions. The literature is, justifiably so, replete with approaches designed for the study of protein interactions. Advances are, nevertheless, highly desirable. An ideal isolation would maintain the protein complex or a larger assembly of interest as close as possible to its original state in the cell. To date, achieving this ideal isolation remains a challenge. The identification of transient or weak interacting partners and the stoichiometry within a complex present difficulties. We have recently reported an approach for the rapid and efficient isolation of protein complexes. We demonstrated that a combination of cryogenic-based cell lysis and fast immunoaffinity purifications helps to maintain interactions, minimizing nonspecific associations and maximizing the recovery of transiently interacting partners. This presentation will underline some of the technical aspects that were found to be important in studying protein complexes, as well as macromolecular assemblies. Highlights will be shown from our studies of the dynamic viral-host protein interactions during the course of infections with Sindbis and human cytomegalovirus HCMV. Our results revealed cellular pathways utilized by these viruses to manipulate host systems.
http://proteome.nih.gov In case of problems with this stream, there is a backup stream at http://videocast.nih.gov/ram/protig110708.ram |
| Author: | Ileana Cristea, Princeton University |
| Runtime: | 75 minutes |
| CIT File ID: | 14762 |
| CIT Live ID: | 7264 |
| Permanent link: | http://videocast.nih.gov/launch.asp?14762 |