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1. Quantitation of de novo localized (15)N-labeled lipoproteins and membrane proteins having one and two transmembrane segments in a Bacillus subtilis secA temperature-sensitive mutant using 2D-PAGE and MALDI-TOF MS.

Author

Bunai K, Nozaki M, Kakeshita H, Nemoto T, and Yamane K

Subjects
Adenosine Triphosphatases, Bacillus subtilis genetics, Electrophoresis, Gel, Two-Dimensional, Membrane Transport Proteins, Mutation, Nitrogen Isotopes, Protein Transport, SEC Translocation Channels, SecA Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Temperature, Bacillus subtilis chemistry, Bacterial Proteins analysis, Lipoproteins analysis, Membrane Proteins analysis, Proteomics methods
Abstract

We developed a means of quantifying proteins that have just localized in the cytoplasmic membrane using 15N-whole cell labeling together with 2D-PAGE and MALDI-TOF MS. The localization of 18 among 20 proteins consisting of 8 lipoproteins, 11 integral membrane proteins having one or two transmembrane segments and one secretory protein in the membrane fractions of Bacillus subtilis, was inhibited by the absence of SecA in a temperature-sensitive mutant. The time course of inhibition indicated that SecA participates in the localization of those proteins through immediately dependent, delayed dependent, and independent ways.

Published
2005
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