Document Detail


Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography.
MedLine Citation:
PMID:  16814929     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Immobilised metal affinity chromatography (IMAC) is the most widely used technique for single-step purification of recombinant proteins. However, despite its use in the purification of heterologue proteins in the eubacteria Escherichia coli for decades, the presence of native E. coli proteins that exhibit a high affinity for divalent cations such as nickel, cobalt or copper has remained problematic. This is of particular relevance when recombinant molecules are not expressed at high levels or when their overexpression induces that of native bacterial proteins due to pleiotropism and/or in response to stress conditions. Identification of such contaminating proteins is clearly relevant to those involved in the purification of histidine-tagged proteins either at small/medium scale or in high-throughput processes. The work presented here reviews the native proteins from E. coli most commonly co-purified by IMAC, including Fur, Crp, ArgE, SlyD, GlmS, GlgA, ODO1, ODO2, YadF and YfbG. The binding of these proteins to metal-chelating resins can mostly be explained by their native metal-binding functions or their possession of surface clusters of histidine residues. However, some proteins fall outside these categories, implying that a further class of interactions may account for their ability to co-purify with histidine-tagged proteins. We propose a classification of these E. coli native proteins based on their physicochemical, structural and functional properties.
Authors:
Victor Martin Bolanos-Garcia; Owen Richard Davies
Related Documents :
21439479 - Context-based identification of protein-protein interfaces and "hot-spot" residues.
21448279 - Detection of prion protein in urine-derived injectable fertility products by a targeted...
12821199 - Two-step purification of his-tagged nef protein in native condition using heparin and i...
3782369 - Comparison of reversed-phase column materials for high-performance liquid chromatograph...
18273849 - A robust protein host for anchoring chelating ligands and organocatalysts.
11388809 - Overexpression, rapid isolation, and biochemical characterization of escherichia coli s...
19398759 - Active establishment of centromeric cenp-a chromatin by rsf complex.
12744289 - Studies on the amino acid and mineral content of buckwheat protein fractions.
1998709 - Long-term intercalation of residual hemin in erythrocyte membranes distorts the cell.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2006-04-26
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1760     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-09-18     Completed Date:  2006-11-14     Revised Date:  2007-08-13    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1304-13     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, England. victor@cryst.bioc.cam.ac.uk
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Chromatography, Affinity
Escherichia coli / chemistry*,  genetics,  metabolism*
Escherichia coli Proteins / chemistry*,  classification,  isolation & purification,  metabolism*
Humans
Metals / chemistry*,  metabolism*
Models, Molecular
Protein Binding
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Metals

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Diagnostic value of MRI in a pelvic mass of prostatic origin.
Next Document:  Clozapine reverses increased brown adipose tissue thermogenesis induced by 3,4-methylenedioxymethamp...