Proteomics of Corynebacterium glutamicum and Other Corynebacteria
Jörn Kalinowski, Dirk Wolters and Ansgar Poetsch
from: Corynebacteria: Genomics and Molecular Biology (Edited by: Andreas Burkovski). Caister Academic Press, U.K. (2008)
Abstract
Corynebacteria were subject to several proteomics studies in the past, either aiming to describe comprehensive cytosolic, extracellular and membrane proteomes or comparing proteomes of different species, wildtype and mutant strains, respectively. In these surveys, a variety of techniques were applied, one- and two-dimensional gel electrophoresis as well as liquid chromatography (LC) separations. Identification of proteins was done mostly by protease digestion and mass-spectrometry, employing MALDI or ESI mass spectrometers and subsequent comparison of acquired mass spectra with databases. In the next years, automated separation and online identification by LC-MALDI or LC-ESI will progressively replace the gel-based methods, ultimately leading to real quantitative data. While mostly hydrophilic proteins can be analyzed comprehensively with routine techniques, separation and identification of membrane proteins is more complex and was investigated in detail in a number of recent studies. This chapter will first review the initial work on hydrophilic proteins and then focus on membrane proteomics as the novel and fast proceeding field of research read more ...
