MccJ25 C-terminal is involved in RNA-polymerase inhibition but not in respiration inhibition
- 3 June 2005
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 331 (2), 549-551
- https://doi.org/10.1016/j.bbrc.2005.03.220
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- The microcin J25 β-hairpin region is important for antibiotic uptake but not for RNA polymerase and respiration inhibitionBiochemical and Biophysical Research Communications, 2004
- Inhibition ofSalmonella entericaserovars by microcin J25FEMS Microbiology Letters, 2004
- Microcin J25 Has a Threaded Sidechain-to-Backbone Ring Structure and Not a Head-to-Tail Cyclized BackboneJournal of the American Chemical Society, 2003
- Structure of Microcin J25, a Peptide Inhibitor of Bacterial RNA Polymerase, is a Lassoed TailJournal of the American Chemical Society, 2003
- Structure of Antibacterial Peptide Microcin J25: A 21-Residue Lariat ProtoknotJournal of the American Chemical Society, 2003
- Chemical modification of microcin J25 with diethylpyrocarbonate and carbodiimide: evidence for essential histidyl and carboxyl residuesBiochemical and Biophysical Research Communications, 2003
- The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newportFEMS Microbiology Letters, 2001
- Escherichia coli RNA Polymerase Is the Target of the Cyclopeptide Antibiotic Microcin J25Journal of Bacteriology, 2001
- The FhuA protein is involved in microcin 25 uptakeJournal of Bacteriology, 1993
- Microcin 25, a novel antimicrobial peptide produced by Escherichia coliJournal of Bacteriology, 1992