Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein
- 31 December 1991
- journal article
- Published by Elsevier in Research in Microbiology
- Vol. 142 (9), 951-963
- https://doi.org/10.1016/0923-2508(91)90005-u
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Catabolite repression of α amylase gene expression in Bacillus subtilis involves a trans‐acting gene product homologous to the Escherichia coli lacl and galR repressorsMolecular Microbiology, 1991
- Structure and evolution of a multidomain multiphosphoryl transfer proteinJournal of Molecular Biology, 1990
- Consensus methods for finding and ranking DNA binding sitesJournal of Molecular Biology, 1989
- Relationship between pseudo-HPr and the PEP: fructose phosphotransferase system in Salmonella typhimurium and Escherichia coliMolecular Genetics and Genomics, 1986
- Predicted structure of the sugar-binding site of the lac repressorNature, 1984
- Sequence homology between Lac and Gal repressors and three sugar-binding periplasmic proteinsNature, 1983
- [47] Establishing homologies in protein sequencesMethods in Enzymology, 1983
- [2] New M13 vectors for cloningMethods in Enzymology, 1983
- Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes: A proposal for a synonymous codon choice that is optimal for the E. coli translational systemJournal of Molecular Biology, 1981
- Sequence of the lacI geneNature, 1978