CEEPC/IPM/CMSC - Abstrakt prezentace

(3. konference České společnosti pro hmotnostní spektrometrii - PL-1)
Protein interaction topologies in cells: snapshots of the landscape

James E. Bruce 1 *

  1. University of Washington


Protein-protein interactions are essential to all function needed to support life. Highly specific protein structures and topological features have evolved to underpin exceedingly selective protein-protein interactions within complex biological mixtures. Many proteins, often exhibit intended structures only within their predestined subcellular environment. For these, the only opportunity to study interaction topologies may be when these proteins are present in cells. This presentation will describe our efforts to identify protein topological features and protein-protein interactions within native environments in human, yeast, E. coli and other bacterial cells. More than 1000 proteins have been cross-linked in cells and identified using Protein Interaction Reporter (PIR) technology yielding a database of several thousand high confidence PIR-cross-linked peptide pairs from these proteins. Examples to be discussed include proteins with well-studied function not previously known to interact directly with one another in cells (metabolic proteins and proteins within the glycolysis pathway that were observed to be cross-linked). Additionally, membrane proteins form 20 to 25% of the total proteins cross-linked in cells and appear to constitute a unique class of proteins for which PIR technology can yield topological and protein-protein interaction information. Examples of PIR-cross-linked membrane protein complexes will be presented to illustrate how the identified sites enable structure prediction of membrane proteins and their complexes. Finally, this presentation will highlight protein interaction topologies with relevance to antibiotic resistance and pathogenicity in bacteria, chemotherapy and acquired chemoresistance in cancer cells.

* Korespondující autor: jimbruce@u.washington.edu

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