학술논문
A protein complex network of Drosophila melanogaster.
Document Type
Academic Journal
Author
Guruharsha KG; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.; Rual JF; Zhai B; Mintseris J; Vaidya P; Vaidya N; Beekman C; Wong C; Rhee DY; Cenaj O; McKillip E; Shah S; Stapleton M; Wan KH; Yu C; Parsa B; Carlson JW; Chen X; Kapadia B; VijayRaghavan K; Gygi SP; Celniker SE; Obar RA; Artavanis-Tsakonas S
Source
Publisher: Cell Press Country of Publication: United States NLM ID: 0413066 Publication Model: Print Cited Medium: Internet ISSN: 1097-4172 (Electronic) Linking ISSN: 00928674 NLM ISO Abbreviation: Cell Subsets: MEDLINE
Subject
Language
English
Abstract
Determining the composition of protein complexes is an essential step toward understanding the cell as an integrated system. Using coaffinity purification coupled to mass spectrometry analysis, we examined protein associations involving nearly 5,000 individual, FLAG-HA epitope-tagged Drosophila proteins. Stringent analysis of these data, based on a statistical framework designed to define individual protein-protein interactions, led to the generation of a Drosophila protein interaction map (DPiM) encompassing 556 protein complexes. The high quality of the DPiM and its usefulness as a paradigm for metazoan proteomes are apparent from the recovery of many known complexes, significant enrichment for shared functional attributes, and validation in human cells. The DPiM defines potential novel members for several important protein complexes and assigns functional links to 586 protein-coding genes lacking previous experimental annotation. The DPiM represents, to our knowledge, the largest metazoan protein complex map and provides a valuable resource for analysis of protein complex evolution.
(Copyright © 2011 Elsevier Inc. All rights reserved.)
(Copyright © 2011 Elsevier Inc. All rights reserved.)