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Capturing protein communities by structural proteomics in a thermophilic eukaryote

ABSTRACT: The arrangement of proteins into complexes is a key organizational principle for many cellular functions. Although the topology of many complexes has been systematically analyzed in isolation, their molecular sociology in situ remains elusive. Here, we show that crude cellular extracts of a eukaryotic thermophile, Chaetomium thermophilum, retain basic principles of cellular organization. Using a structural proteomics approach, we simultaneously characterized the abundance, interactions and structure of a third of the C. thermophilum proteome within these extracts. We identified 27 distinct protein communities that include 108 interconnected complexes, which dynamically associate with each other and functionally benefit from being in close proximity in the cell.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Chaetomium Thermophilum

SUBMITTER: Katarzyna Buczak

LAB HEAD: Martin Beck

PROVIDER: PXD006660 | Pride | 2017-08-07

REPOSITORIES: Pride

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Capturing protein communities by structural proteomics in a thermophilic eukaryote.

Kastritis Panagiotis L PL O'Reilly Francis J FJ Bock Thomas T Li Yuanyue Y Rogon Matt Z MZ Buczak Katarzyna K Romanov Natalie N Betts Matthew J MJ Bui Khanh Huy KH Bui Khanh Huy KH Hagen Wim J WJ Hennrich Marco L ML Mackmull Marie-Therese MT Rappsilber Juri J Russell Robert B RB Russell Robert B RB Bork Peer P Beck Martin M Gavin Anne-Claude AC

Molecular systems biology 20170725 7

The arrangement of proteins into complexes is a key organizational principle for many cellular functions. Although the topology of many complexes has been systematically analyzed in isolation, their molecular sociology <i>in situ</i> remains elusive. Here, we show that crude cellular extracts of a eukaryotic thermophile, <i>Chaetomium thermophilum</i>, retain basic principles of cellular organization. Using a structural proteomics approach, we simultaneously characterized the abundance, interact ...[more]

PMID: 28743795

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