Maltotriose is the inducer of the maltose regulon of Escherichia coli
- 1 July 1987
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 169 (7) , 3059-3061
- https://doi.org/10.1128/jb.169.7.3059-3061.1987
Abstract
In a cell-free system programmed with a plasmid bearing a malP'-'lacZ gene fusion under the control of malPp, beta-galactosidase synthesis was strictly dependent on the presence of both the MalT activator protein and the inducer of the Escherichia coli maltose regulon. We show that, among all maltodextrins tested (from maltose to maltoheptaose), only maltotriose was able to induce beta-galactosidase synthesis. Likewise, in an in vitro transcription system, initiation of transcription at malPp required the presence of the MalT protein and maltotriose along with the RNA polymerase holoenzyme; neither maltose nor maltotetraose could substitute for maltotriose.This publication has 19 references indexed in Scilit:
- POSITIVE CONTROL OF TRANSCRIPTION INITIATION IN BACTERIAAnnual Review of Genetics, 1984
- The Recognition of Maltodextrins by Escherichia coliEuropean Journal of Biochemistry, 1980
- Synthesis and maturation of lambda receptor in Escherichia coli K-12: in vivo and in vitro expression of gene lamB under lac promoter control.Proceedings of the National Academy of Sciences, 1980
- Dominant constitutive mutations in malT, the positive regulator gene of the maltose regulon in Escherichia coliJournal of Molecular Biology, 1978
- The use of thin acrylamide gels for DNA sequencingFEBS Letters, 1978
- The Action Pattern of Amylomaltase from Escherichia coliEuropean Journal of Biochemistry, 1976
- Maltose Transport in Escherichia coli K12. A Comparison of Transport Kinetics in Wild-Type and lamba-Resistant Mutants with the Dissociation Constants of the Maltose-Binding Protein as Measured by Fluorescence QuenchingEuropean Journal of Biochemistry, 1976
- Regulation of the l-Arabinose Operon BAD in VitroJournal of Biological Chemistry, 1974
- The Pathway of Exogenous and Endogenous Carbohydrate Utilization in Escherichia coli: A Dual Function for the Enzymes of the Maltose OperonEuropean Journal of Biochemistry, 1973
- La maltodextrine phosphorylase d' Escherichia coliEuropean Journal of Biochemistry, 1967