Difference between revisions of "PMID:4359648"

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'''Ordal, GW and Adler, J'''  (1974) Properties of mutants in galactose taxis and transport. ''J. Bacteriol.'' '''117''':517-26
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!align=left align='left' bgcolor='#CCCCFF' |Abstract
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beta-Methylgalactoside (mgl) permease mutants of Escherichia coli, which are defective in three genes, mglA, mglB, and mglC, were assayed for galactose taxis and galactose transport. The mglB product is the galactose-binding protein. Previous evidence, supported by our new findings, shows that the galactose-binding protein is the recognition component for galactose taxis as well as for galactose transport. Most mutants defective in mglB showed strong effects on both chemotaxis and transport; however, a couple showed effects chiefly on one process or the other, thus allowing a separation of chemotaxis and transport. The mglA and mglC products have not yet been identified, but they must be components of the galactose transport machinery since mutants defective in mglA or mglC, or both, showed strongly reduced transport. Although some of these mutants showed little chemotaxis, most gave close to wild-type chemotactic responses. Thus, transport is not required for galactose taxis. The bacteria detect changes in the fraction of binding protein associated with galactose, not changes in the rate of transport.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4359648 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC285542 PMC285542]
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!align=left align='left' bgcolor='#CCCCFF' |Keywords
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Bacterial Proteins/metabolism; Biological Transport, Active; Carbon Radioisotopes; Chemotaxis; Escherichia coli/enzymology; Escherichia coli/metabolism; Galactose/metabolism; Genes; Membrane Transport Proteins/biosynthesis; Methylglycosides; Micropore Filters; Mutation; Phosphotransferases/biosynthesis; Protein Binding
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==Main Points of the Paper ==
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== Materials and Methods Used ==
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==Phenotype Annotations==
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==Notes==
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==References==
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[[Category:Publication]]

Latest revision as of 15:38, 29 June 2015

Citation

Ordal, GW and Adler, J (1974) Properties of mutants in galactose taxis and transport. J. Bacteriol. 117:517-26

Abstract

beta-Methylgalactoside (mgl) permease mutants of Escherichia coli, which are defective in three genes, mglA, mglB, and mglC, were assayed for galactose taxis and galactose transport. The mglB product is the galactose-binding protein. Previous evidence, supported by our new findings, shows that the galactose-binding protein is the recognition component for galactose taxis as well as for galactose transport. Most mutants defective in mglB showed strong effects on both chemotaxis and transport; however, a couple showed effects chiefly on one process or the other, thus allowing a separation of chemotaxis and transport. The mglA and mglC products have not yet been identified, but they must be components of the galactose transport machinery since mutants defective in mglA or mglC, or both, showed strongly reduced transport. Although some of these mutants showed little chemotaxis, most gave close to wild-type chemotactic responses. Thus, transport is not required for galactose taxis. The bacteria detect changes in the fraction of binding protein associated with galactose, not changes in the rate of transport.

Links

PubMed PMC285542

Keywords

Bacterial Proteins/metabolism; Biological Transport, Active; Carbon Radioisotopes; Chemotaxis; Escherichia coli/enzymology; Escherichia coli/metabolism; Galactose/metabolism; Genes; Membrane Transport Proteins/biosynthesis; Methylglycosides; Micropore Filters; Mutation; Phosphotransferases/biosynthesis; Protein Binding

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Main Points of the Paper

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Materials and Methods Used

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Phenotype Annotations

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Phenotype of Taxon Information Genotype Information (if known) Condition Information OMP ID OMP Term Name ECO ID ECO Term Name Notes Status
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</protect>

Notes

References

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