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Proteome of the Bacterium Mycoplasma gallisepticum

I. A. Demina1*, M. V. Serebryakova1, V. G. Ladygina1, M. A. Rogova1, V. G. Zgoda2, D. A. Korzhenevskyi1, and V. M. Govorun1

1Research Institute for Physical-Chemical Medicine, Ministry of Public Health of the Russian Federation, ul. Malaya Pirogovskaya 1a, 119992 Moscow, Russia; fax: (495) 246-4401; E-mail: idemina@mail.ru

2Orekhovich Research Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, ul. Pogodinskaya 10, 119121 Moscow, Russia; fax: (495) 245-0857

* To whom correspondence should be addressed.

Received June 6, 2008; Revision received August 14, 2008
Using modern proteomic assays, we have identified the products of gene expression and posttranslational modifications of proteins of the bacterium Mycoplasma gallisepticum S6. Combinations of different technologies of protein separation by electrophoresis and mass-spectrometric analysis gave us a total of 446 proteins, i.e. 61% of the annotated proteins of this microorganism. The Pro-Q Diamond and Pro-Q Emerald dye technology was used for fluorescent detection of ten phosphoproteins and two glycoproteins. The acylation of proteins was studied by electrophoresis after in vivo labeling with different 14C-labeled fatty acids, followed by autoradiography. Sixteen acylated proteins were identified, with a quarter of them involved in plasma membrane construction and another quarter involved in cell energy metabolism.
KEY WORDS: Mycoplasma gallisepticum, proteomics, 2-D electrophoresis, mass spectrometry, posttranslational modifications

DOI: 10.1134/S0006297909020072