scholarly journals Data-directed top-down Fourier-transform mass spectrometry of a large integral membrane protein complex: Photosystem II from Galdieria sulphuraria

PROTEOMICS ◽  
2010 ◽  
Vol 10 (20) ◽  
pp. 3644-3656 ◽  
Author(s):  
Balakumar Thangaraj ◽  
Christopher M. Ryan ◽  
Puneet Souda ◽  
Kirsten Krause ◽  
Kym F. Faull ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fourier Transform ◽  
Photosystem Ii ◽  
Membrane Protein ◽  
Protein Complex ◽  
Fourier Transform Mass Spectrometry ◽  
Integral Membrane Protein ◽  
Galdieria Sulphuraria ◽  
Top Down ◽  
Membrane Protein Complex

scholarly journals Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding

2016 ◽  
Vol 113 (29) ◽  
pp. 8230-8235 ◽  
Author(s):  
Idlir Liko ◽  
Matteo T. Degiacomi ◽  
Shabaz Mohammed ◽  
Shinya Yoshikawa ◽  
Carla Schmidt ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Posttranslational Modifications ◽  
Protein Complex ◽  
Integral Membrane Protein ◽  
Intact Protein ◽  
Oligomeric State ◽  
Membrane Protein Complex ◽  
Dimer Interface ◽  
Lipid Species

Bovine cytochrome c oxidase is an integral membrane protein complex comprising 13 protein subunits and associated lipids. Dimerization of the complex has been proposed; however, definitive evidence for the dimer is lacking. We used advanced mass spectrometry methods to investigate the oligomeric state of cytochrome c oxidase and the potential role of lipids and posttranslational modifications in its subunit interfaces. Mass spectrometry of the intact protein complex revealed that both the monomer and the dimer are stabilized by large lipid entities. We identified these lipid species from the purified protein complex, thus implying that they interact specifically with the enzyme. We further identified phosphorylation and acetylation sites of cytochrome c oxidase, located in the peripheral subunits and in the dimer interface, respectively. Comparing our phosphorylation and acetylation sites with those found in previous studies of bovine, mouse, rat, and human cytochrome c oxidase, we found that whereas some acetylation sites within the dimer interface are conserved, suggesting a role for regulation and stabilization of the dimer, phosphorylation sites were less conserved and more transient. Our results therefore provide insights into the locations and interactions of lipids with acetylated residues within the dimer interface of this enzyme, and thereby contribute to a better understanding of its structure in the natural membrane. Moreover dimeric cytochrome c oxidase, comprising 20 transmembrane, six extramembrane subunits, and associated lipids, represents the largest integral membrane protein complex that has been transferred via electrospray intact into the gas phase of a mass spectrometer, representing a significant technological advance.

scholarly journals Micro-heterogeneity of human saliva peptide P-C characterized by high-resolution top-down fourier-transform mass spectrometry

2010 ◽  
Vol 21 (5) ◽  
pp. 868-877 ◽  
Author(s):  
Frédéric Halgand ◽  
Vlad Zabrouskov ◽  
Sara Bassilian ◽  
Puneet Souda ◽  
David T. Wong ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fourier Transform ◽  
High Resolution ◽  
Fourier Transform Mass Spectrometry ◽  
Human Saliva ◽  
Top Down

Top-Down Approaches for Measuring Expression Ratios of Intact Yeast Proteins Using Fourier Transform Mass Spectrometry

2006 ◽  
Vol 78 (3) ◽  
pp. 686-694 ◽  
Author(s):  
Yi Du ◽  
Bryan A. Parks ◽  
Seyoung Sohn ◽  
Kurt E. Kwast ◽  
Neil L. Kelleher
Keyword(s):  
Mass Spectrometry ◽  
Fourier Transform ◽  
Fourier Transform Mass Spectrometry ◽  
Top Down
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