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Title | Capturing protein communities by structural proteomics in a thermophilic eukaryote. |
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Journal, issue, pages | Mol Syst Biol, Vol. 13, Issue 7, Page 936, Year 2017 |
Publish date | Jul 25, 2017 |
Authors | Panagiotis L Kastritis / Francis J O'Reilly / Thomas Bock / Yuanyue Li / Matt Z Rogon / Katarzyna Buczak / Natalie Romanov / Matthew J Betts / Khanh Huy Bui / Wim J Hagen / Marco L Hennrich / Marie-Therese Mackmull / Juri Rappsilber / Robert B Russell / Peer Bork / Martin Beck / Anne-Claude Gavin / |
PubMed 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 ...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 remains elusive. Here, we show that crude cellular extracts of a eukaryotic thermophile, , retain basic principles of cellular organization. Using a structural proteomics approach, we simultaneously characterized the abundance, interactions, and structure of a third of the 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. Furthermore, we investigated the structure of fatty acid synthase within these extracts by cryoEM and this revealed multiple, flexible states of the enzyme in adaptation to its association with other complexes, thus exemplifying the need for studies. As the components of the captured protein communities are known-at both the protein and complex levels-this study constitutes another step forward toward a molecular understanding of subcellular organization. |
External links | Mol Syst Biol / PubMed:28743795 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.7 Å |
Structure data | EMDB-3757: |
Source |
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