Mapping phosphoproteins in <Emphasis Type="Italic">Mycoplasma genitalium</Emphasis> and <Emphasis Type="Italic">Mycoplasma pneumoniae</Emphasis> |
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| Authors: | Hsun-Cheng Su III" target="_blank">Clyde A HutchisonIII Morgan C Giddings |
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| Institution: | (1) Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, 27599, NC, USA;(2) J. Craig Venter Institute, 20850 Rockville, MD, USA;(3) Joint Department of Biomedical Engineering, University of North Carolina at Chapel Hill, 27599 Chapel Hill, NC, USA;(4) North Carolina State University, 27695 Raleigh, NC, USA;(5) Department of Computer Science, University of North Carolina at Chapel Hill, 27599 Chapel Hill, NC, USA |
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| Abstract: | Background Little is known regarding the extent or targets of phosphorylation in mycoplasmas, yet in many other bacterial species phosphorylation
is known to play an important role in signaling and regulation of cellular processes. To determine the prevalence of phosphorylation
in mycoplasmas, we examined the CHAPS-soluble protein fractions of Mycoplasma genitalium and Mycoplasma pneumoniae by two-dimensional gel electrophoresis (2-DE), using a combination of Pro-Q Diamond phosphoprotein stain and 33P labeling. Protein spots that were positive for phosphorylation were identified by peptide mass fingerprinting using MALDI-TOF-TOF
mass spectrometry. |
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