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Large-scale identification of protein–protein interaction of Escherichia coli K-12

2006; Cold Spring Harbor Laboratory Press; Volume: 16; Issue: 5 Linguagem: Inglês

10.1101/gr.4527806

1549-5469

Mohammad Arifuzzaman, Maki Maeda, Aya Itoh, Kensaku Nishikata, Chiharu Takita, Rintaro Saito, Takeshi Ara, Kenji Nakahigashi, Hsuan‐Cheng Huang, Aki Hirai, Kohei Tsuzuki, Seira Nakamura, Mohammad Altaf-Ul-Amin, Taku Oshima, Tomoya Baba, Natsuko Yamamoto, Tomoyo Kawamura, Tomoko Ioka-Nakamichi, Masanari Kitagawa, Masaru Tomita, Shigehiko Kanaya, Chieko Wada, Hirotada Mori,

Fungal and yeast genetics research

Protein–protein interactions play key roles in protein function and the structural organization of a cell. A thorough description of these interactions should facilitate elucidation of cellular activities, targeted-drug design, and whole cell engineering. A large-scale comprehensive pull-down assay was performed using a His-tagged Escherichia coli ORF clone library. Of 4339 bait proteins tested, partners were found for 2667, including 779 of unknown function. Proteins copurifying with hexahistidine-tagged baits on a Ni 2+ -NTA column were identified by MALDI-TOF MS (matrix-assisted laser desorption ionization time of flight mass spectrometry). An extended analysis of these interacting networks by bioinformatics and experimentation should provide new insights and novel strategies for E. coli systems biology.