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Global analysis of the Deinococcus radiodurans proteome by using accurate mass tags

2002; National Academy of Sciences; Volume: 99; Issue: 17 Linguagem: Inglês

10.1073/pnas.172170199

1091-6490

Mary Lipton, Ljiljana Paša‐Tolić, Gordon Anderson, David J. Anderson, Deanna L. Auberry, John R. Battista, Michael J. Daly, Jim Fredrickson, Kim Hixson, Heather M. Kostandarithes, Christophe Masselon, Lye Meng Markillie, Ronald J. Moore, Margaret F. Romine, Yufeng Shen, Eric Stritmatter, Nikola Tolić, Harold R. Udseth, Amudhan Venkateswaran, Kwong‐Kwok Wong, Rui Zhao, Richard Smith,

Genomics and Phylogenetic Studies

Understanding biological systems and the roles of their constituents is facilitated by the ability to make quantitative, sensitive, and comprehensive measurements of how their proteome changes, e.g., in response to environmental perturbations. To this end, we have developed a high-throughput methodology to characterize an organism's dynamic proteome based on the combination of global enzymatic digestion, high-resolution liquid chromatographic separations, and analysis by Fourier transform ion cyclotron resonance mass spectrometry. The peptides produced serve as accurate mass tags for the proteins and have been used to identify with high confidence >61% of the predicted proteome for the ionizing radiation-resistant bacterium Deinococcus radiodurans . This fraction represents the broadest proteome coverage for any organism to date and includes 715 proteins previously annotated as either hypothetical or conserved hypothetical.