NDLI: The Escherichia coli peripheral inner membrane proteome.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Papanastasiou, Malvina Orfanoudaki, Georgia Koukaki, Marina Kountourakis, Nikos Sardis, Marios Frantzeskos Aivaliotis, Michalis Karamanou, Spyridoula Economou, Anastassios
Description	Country affiliation: Greece Author Affiliation: Papanastasiou M ( Institute of Molecular Biology and Biotechnology-FORTH, Iraklio, Crete, Greece.)
Abstract	Biological membranes are essential for cell viability. Their functional characteristics strongly depend on their protein content, which consists of transmembrane (integral) and peripherally associated membrane proteins. Both integral and peripheral inner membrane proteins mediate a plethora of biological processes. Whereas transmembrane proteins have characteristic hydrophobic stretches and can be predicted using bioinformatics approaches, peripheral inner membrane proteins are hydrophilic, exist in equilibria with soluble pools, and carry no discernible membrane targeting signals. We experimentally determined the cytoplasmic peripheral inner membrane proteome of the model organism Escherichia coli using a multidisciplinary approach. Initially, we extensively re-annotated the theoretical proteome regarding subcellular localization using literature searches, manual curation, and multi-combinatorial bioinformatics searches of the available databases. Next we used sequential biochemical fractionations coupled to direct identification of individual proteins and protein complexes using high resolution mass spectrometry. We determined that the proposed cytoplasmic peripheral inner membrane proteome occupies a previously unsuspected â¼19% of the basic E. coli BL21(DE3) proteome, and the detected peripheral inner membrane proteome occupies â¼25% of the estimated expressed proteome of this cell grown in LB medium to mid-log phase. This value might increase when fleeting interactions, not studied here, are taken into account. Several proteins previously regarded as exclusively cytoplasmic bind membranes avidly. Many of these proteins are organized in functional or/and structural oligomeric complexes that bind to the membrane with multiple interactions. Identified proteins cover the full spectrum of biological activities, and more than half of them are essential. Our data suggest that the cytoplasmic proteome displays remarkably dynamic and extensive communication with biological membrane surfaces that we are only beginning to decipher.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
DOI	10.1074/mcp.M112.024711
Journal	Molecular & Cellular Proteomics
Issue Number	3
Volume Number	12
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2013-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics Cell Membrane Metabolism Escherichia Coli Proteins Escherichia Coli Proteome Proteomics Chromatography, Liquid Membrane Proteins Nanotechnology Tandem Mass Spectrometry Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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