Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes.

ABSTRACT: The membrane proteome plays a critical role in electron transport processes in Shewanella oneidensis MR-1, a bacterial organism that has great potential for bioremediation. Biotinylation of intact cells with subsequent affinity-enrichment has become a useful tool for characterization of the membrane proteome. As opposed to these commonly used, water-soluble commercial reagents, we here introduce a family of hydrophobic, cell-permeable affinity probes for extensive labeling and detection of membrane proteins. When applied to S. oneidensis cells, all three new chemical probes allowed identification of a substantial proportion of membrane proteins from total cell lysate without the use of specific membrane isolation method. From a total of 410 unique proteins identified, approximately 42% are

SUBMITTER: Tang X 

PROVIDER: S-EPMC2527595 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature