Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.

Journal article

The ability of electrospray to propel large viruses into a mass spectrometer is established and is rationalized by analogy to the atmospheric transmission of the common cold. Much less clear is the fate of membrane-embedded molecular machines in the gas phase. Here we show that rotary adenosine triphosphatases (ATPases)/synthases from Thermus thermophilus and Enterococcus hirae can be maintained intact with membrane and soluble subunit interactions preserved in vacuum. Mass spectra reveal sub...

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Authors: Zhou, M; Morgner, N; Politis, A; Isaacson, S; Matak-Vinković, D

• Publication status: Published
• Journal: Science (New York, N.Y.)
• Volume: 334
• Issue: 6054
• Pages: 380-385
• Publication date: 2011-10-01
• DOI: 10.1126/science.1210148
• EISSN: 1095-9203
• ISSN: 0036-8075
• Language: English
• Keywords: Binding Sites; Cardiolipins; Models, Molecular; Adenosine Triphosphate; Hydrophobic and Hydrophilic Interactions; Protein Conformation; Phosphatidylethanolamines; Protein Multimerization; Hydrolysis; Thermus thermophilus; Protein Subunits; Membrane Lipids; Enterococcus; Mass Spectrometry; Bacterial Proteins; Adenosine Triphosphatases; Protein Structure, Tertiary; Spectrometry, Mass, Electrospray Ionization; Vacuolar Proton-Translocating ATPases