Change search
ReferencesLink to record
Permanent link

Direct link
Global organization of protein complexome in the yeast Saccharomyces cerevisiae
Umeå University, Faculty of Science and Technology, Department of Physics. (IceLab)
Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, USA.
Institute for the BioCentury and Department of Physics, Korea Advanced Institute of Science and Technology, Korea.
2011 (English)In: BMC Systems Biology, ISSN 1752-0509, Vol. 5, no 126, 15- p.Article in journal (Refereed) Published
Abstract [en]

Background: Proteins in organisms, rather than act alone, usually form protein complexes to perform cellular functions. We analyze the topological network structure of protein complexes and their component proteins in the budding yeast in terms of the bipartite network and its projections, where the complexes and proteins are its two distinct components. Compared to conventional protein-protein interaction networks, the networks from the protein complexes show more homogeneous structures than those of the binary protein interactions, implying the formation of complexes that cause a relatively more uniform number of interaction partners. In addition, we suggest a new optimization method to determine the abundance and function of protein complexes, based on the information of their global organization. Estimating abundance and biological functions is of great importance for many researches, by providing a quantitative description of cell behaviors, instead of just a "catalogues" of the lists of protein interactions.

Results: With our new optimization method, we present genome-wide assignments of abundance and biological functions for complexes, as well as previously unknown abundance and functions of proteins, which can provide significant information for further investigations in proteomics. It is strongly supported by a number of biologically relevant examples, such as the relationship between the cytoskeleton proteins and signal transduction and the metabolic enzyme Eno2's involvement in the cell division process.

Conclusions: We believe that our methods and findings are applicable not only to the specific area of proteomics, but also to much broader areas of systems biology with the concept of optimization principle.

Place, publisher, year, edition, pages
BioMed Central , 2011. Vol. 5, no 126, 15- p.
National Category
Bioinformatics (Computational Biology)
URN: urn:nbn:se:umu:diva-45963DOI: 10.1186/1752-0509-5-126OAI: diva2:436593
Available from: 2011-08-24 Created: 2011-08-24 Last updated: 2011-09-29Bibliographically approved

Open Access in DiVA

fulltext(914 kB)118 downloads
File information
File name FULLTEXT02.pdfFile size 914 kBChecksum SHA-512
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Search in DiVA

By author/editor
Lee, Sang Hoon
By organisation
Department of Physics
In the same journal
BMC Systems Biology
Bioinformatics (Computational Biology)

Search outside of DiVA

GoogleGoogle Scholar
Total: 118 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 53 hits
ReferencesLink to record
Permanent link

Direct link