Journal
JOURNAL OF PROTEOME RESEARCH
Volume 7, Issue 11, Pages 5033-5039Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr800517a
Keywords
Proteome; Archaea; haloarchaea; halophile
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Funding
- NIH [R01 GM057498]
- DOE [DE-FG02-05ER15650, DE-FG02-91ER20041]
- NSF [MCB 0620005]
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Haloferax volcanii, an extreme halophile originally isolated from the Dead Sea, is used worldwide as a model organism for furthering our understanding of archaeal cell physiology. In this study, a combination of approaches was used to identify a total of 1296 proteins, representing 32% of the theoretical proteome of this haloarchaeon. This included separation of (phospho)proteins/peptides by 2-dimensional gel electrophoresis (2-D), immobilized metal affinity chromatography (IMAC), metal oxide affinity chromatography (MOAC), and Multidimensional Protein Identification Technology (MudPIT) including strong cation exchange (SCX) chromatography coupled with reversed phase (RP) HPLC. Proteins were identified by tandem mass spectrometry (MS/MS) using nanoelectrospray ionization hybrid quadrupole time-of-flight (QSTAR XL Hybrid LC/MS/MS System) and quadrupole ion trap (Thermo LCQ Deca). Results indicate that a SCX RP HPLC fractionation coupled with MS/MS provides the best high-throughput workflow for overall protein identification.
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