ArticleProtein science : a publication of the Protein Society1996
The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Characterizing the Conformational Dynamics of the Ribose Transporter B Protein inJournal of chemical theory and computation · 2026Article
- High-throughput, signature-tagged mutagenic approach to identify novel virulence factors of Yersinia pestis CO92 in a mouse model of infection.Infection and immunity · 2015Article
- In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.The Journal of biological chemistry · 2015Article
- The motor domains of ABC-transporters. What can structures tell us?Naunyn-Schmiedeberg's archives of pharmacology · 2006Review
- Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coli.The Biochemical journal · 2005Article
- Topology of RbsC, the membrane component of the Escherichia coli ribose transporter.Journal of bacteriology · 2003Article
- Topology of RbsC, a membrane component of the ribose transporter, belonging to the AraH superfamily.Journal of bacteriology · 1999Article
- Linkage map of Escherichia coli K-12, edition 10: the traditional map.Microbiology and molecular biology reviews : MMBR · 1998Review
- The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA.Protein science : a publication of the Protein Society · 1996Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.