NDLI: The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC.

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The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA.

The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC.

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The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhang, H. Binnie, R. A. Hermodson, M. Zaitseva, J.
Description	Country affiliation: United States Author Affiliation: Zaitseva J ( Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-1153, USA.)
Abstract	Chimeric genes encoding full-length copies of rbsA and rbsC connected by segments coding for short bridge peptides were constructed and expressed in Escherichia coli. Surprisingly, the chimeric genes complemented the strain in which rbsA and rbsC were deleted. The chimeric proteins were overproduced, and the products were purified by affinity chromatography. In order to obtain highly purified protein, a poly-His leader peptide was incorporated so that Ni-chelate affinity chromatography could be employed. The leader peptide and the bridge peptide were designed with factor Xa-cleavable sites to permit recovery of the individual RbsA and RbsC protein. A rbsC gene encoding a poly-His leader was also constructed and expressed. Both the chimeric RbsA-C species and the poly-HisRbsC were produced at levels that permitted isolation of the equivalent of milligram quantities of RbsC per liter of culture. This is a substantial increase in amounts from any previous RbsC production vectors. All proteins from the rbs operon have now been overproduced and substantially purified.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Atp-binding Cassette Transporters Isolation & Purification Escherichia Coli Proteins Membrane Transport Proteins Operon Recombinant Fusion Proteins Genetics Chemistry Metabolism Adenosine Analogs & Derivatives Adenosine Triphosphatases Adenosine Triphosphate Affinity Labels Amino Acid Sequence Animals Blotting, Western Carrier Proteins Immunology Chromatography, Affinity Dna, Bacterial Escherichia Coli Enzymology Gene Expression Molecular Sequence Data Mutagenesis, Site-directed Plasmids Rabbits Recombinant Proteins Comparative Study Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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