Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli.


Abstract

It has been proposed (Randall, L. L., and Hardy, S. J. S. (1986) Cell 46, 921-928) that export of protein involves a kinetic partitioning between the pathway that leads to productive export and the pathway that leads to the folding of polypeptides into a stable conformation that is incompatible with export. As predicted from this model, a decrease in the rate of export of maltose-binding protein to the periplasmic space in Escherichia coli resulting from a defect in the leader sequence was able to be partially overcome by a mutation that slowed the folding of the precursor, thereby increasing the time in which the polypeptide was competent for export. (Liu, G., Topping, T. B., Cover, W. H., and Randall, L. L. (1988) J. Biol. Chem. 263, 14790-14793). Here we describe mutations of the gene encoding ribose-binding protein that were selected as suppressors of a defect in export of that protein and that alter the folding pathway. We propose that selection of such suppressors may provide a general method to obtain mutations that affect the folding properties of any protein that can be expressed and exported in E. coli. Study holds ProTherm entries: 5158, 5159, 5160 Extra Details: stable conformation; maltose-binding protein; precursor;,folding pathway

Submission Details

ID: XabcJ6Rk

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:28 p.m.

Version: 1

Publication Details
Teschke CM;Kim J;Song T;Park S;Park C;Randall LL,J. Biol. Chem. (1991) Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. PMID:1904869
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2DRI 1995-01-26 1.6 PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS
2GX6 2007-03-20 1.97 Rational stabilization of E. coli ribose binding protein
1DRK 1995-01-26 2.0 PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE-BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS
1BA2 1998-07-15 2.1 D67R MUTANT OF D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI
1DBP 1994-05-31 2.2 IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS
1URP 1998-06-17 2.3 D-RIBOSE-BINDING PROTEIN FROM ESCHERICHIA COLI
1DRJ 1995-01-26 2.5 PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE-BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
97.3 Ribose import binding protein RbsB P0A2C5 RBSB_SALTY
97.3 Ribose import binding protein RbsB P0A2C6 RBSB_SALTI
100.0 Ribose import binding protein RbsB P02925 RBSB_ECOLI