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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1126/science.1210148

Authors


Morgner, N More by this author
Barrera, NP More by this author
Politis, A More by this author
Isaacson, SC More by this author
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Journal:
Science (New York, N.Y.)
Volume:
334
Issue:
6054
Pages:
380-385
Publication date:
2011-10-05
DOI:
EISSN:
1095-9203
ISSN:
0036-8075
URN:
uuid:45ba284d-19ae-4d0b-ac05-8bf59bf5149e
Source identifiers:
193036
Local pid:
pubs:193036

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