Novel Fluorescence Labeling and High-Throughput Assay Technologies for In Vitro Analysis of Protein Interactions | Zendy

Nobuhide Doi | Zendy; Hideaki Takashima | Zendy; Masataka Kinjo | Zendy; Kyoko Sakata | Zendy; Yuko Kawahashi | Zendy; Yuko Oishi | Zendy; Rieko Oyama | Zendy; Etsuko MiyamotoSato | Zendy; Tatsuya Sawasaki | Zendy; Yaeta Endo | Zendy; Hiroshi Yanagawa | Zendy

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Novel Fluorescence Labeling and High-Throughput Assay Technologies for In Vitro Analysis of Protein Interactions

Author(s) -

Nobuhide Doi,

Hideaki Takashima,

Masataka Kinjo,

Kyoko Sakata,

Yuko Kawahashi,

Yuko Oishi,

Rieko Oyama,

Etsuko MiyamotoSato,

Tatsuya Sawasaki,

Yaeta Endo,

Hiroshi Yanagawa

Publication year - 2002

Publication title -

genome research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.556

H-Index - 297

eISSN - 1549-5469

pISSN - 1088-9051

DOI - 10.1101/gr.218802

Subject(s) - fluorophore , biology , fluorescence , computational biology , protein microarray , in vitro , linker , protein–protein interaction , biochemistry , dna , dna microarray , high throughput screening , microbiology and biotechnology , biophysics , gene , gene expression , physics , quantum mechanics , computer science , operating system

We developed and tested a simple method for fluorescence labeling and interaction analysis of proteins based on a highly efficient in vitro translation system combined with high-throughput technologies such as microarrays and fluorescence cross-correlation spectroscopy (FCCS). By use of puromycin analogs linked to various fluorophores through a deoxycytidylic acid linker, a single fluorophore can be efficiently incorporated into a protein at the carboxyl terminus during in vitro translation. We confirmed that the resulting fluorescently labeled proteins are useful for probing protein-protein and protein-DNA interactions by means of pulldown assay, DNA microarrays, and FCCS in model experiments. These fluorescence assay systems can be easily extended to highly parallel analysis of protein interactions in studies of functional genomics.

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