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Mass Spectrom Rev. 2003 Jan-Feb;22(1):27-56.

Subcellular proteomics.

Author information

  • Institute for Chemistry/Biochemistry, Free University Berlin, Thielallee 63, 14195 Berlin, Germany. saihtam@chemie.fu-berlin.de

Abstract

The step from the analysis of the genome to the analysis of the proteome is not just a matter of numerical complexity in terms of variants of gene products that can arise from a single gene. A significant further level of complexity is introduced by the supramolecular organization of gene products because of protein-protein interactions or targeting of proteins to specific subcellular structures. There is currently no single proteome analysis strategy that can sufficiently address all levels of the organization of the proteome. To approach an appropriate analytical complement for the interrogation of the proteome at all of the levels at which it is organized, there emerges the need for a whole arsenal of proteomics strategies. The proteome analysis at the level of subcellular structures (that can be enriched by subcellular fractionation) represents an analytical strategy that combines classic biochemical fractionation methods and tools for the comprehensive identification of proteins. Among the key potentials of this strategy is the capability to screen not only for previously unknown gene products but also to assign them, along with other known, but poorly characterized gene products, to particular subcellular structures. Furthermore, the analysis at the subcellular level is a prerequisite for the detection of important regulatory events such as protein translocation in comparative studies. This review is meant to give an overview on recent key studies in the field of proteome analysis at the level of subcellular structures, and to highlight potentials and requirements.

Copyright 2003 Wiley Periodicals, Inc., Mass Spec Rev 22:27-56, 2003; Published online in Wiley InterScience (www.interscience.wiley.com)

PMID:
12768603
[PubMed - indexed for MEDLINE]
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