A General System for Studying Protein−Protein Interactions in Gram-Negative Bacteria

One of the most promising methods for large-scale studies of protein interactions is isolation of an affinity-tagged protein with its in vivo interaction partners, followed by mass spectrometric identification of the copurified proteins. Previous studies have generated affinity-tagged proteins using...

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Veröffentlicht in:	Journal of proteome research 2008-08, Vol.7 (8), p.3319-3328
Hauptverfasser:	Pelletier, Dale A, Hurst, Gregory B, Foote, Linda J, Lankford, Patricia K, McKeown, Catherine K, Lu, Tse-Yuan, Schmoyer, Denise D, Shah, Manesh B, Hervey, W. Judson, McDonald, W. Hayes, Hooker, Brian S, Cannon, William R, Daly, Don S, Gilmore, Jason M, Wiley, H. Steven, Auberry, Deanna L, Wang, Yisong, Larimer, Frank W, Kennel, Stephen J, Doktycz, Mitchel J, Morrell-Falvey, Jennifer L, Owens, Elizabeth T, Buchanan, Michelle V
Format:	Artikel
Sprache:	eng
Schlagworte:	AFFINITY Affinity Labels BACTERIA Bacterial Proteins - genetics Bacterial Proteins - metabolism BASIC BIOLOGICAL SCIENCES BEARINGS CLONING Cloning, Molecular CMCS DNA-Directed RNA Polymerases - genetics DNA-Directed RNA Polymerases - metabolism ESCHERICHIA COLI Escherichia coli - enzymology Genetic Vectors GENETICS Gram-Negative Bacteria - metabolism IN VIVO Molecular Probes PLASMIDS Protein Interaction Mapping Protein Subunits - genetics Protein Subunits - metabolism PROTEINS Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RECOMBINATION RHODOPSEUDOMONAS Rhodopseudomonas - enzymology RNA POLYMERASES Shewanella - enzymology VECTORS
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