Autogenous Regulation of the Escherichia Coli KsgA Gene at the Level of Translation
Overview
Authors
Affiliations
Various plasmids that contain the Escherichia coli ksgA gene, which encodes a 16S rRNA adenosine dimethyltransferase (methylase), were constructed. In one of these plasmids, the DNA encoding the N-terminal part of the methylase was fused to the lacZ gene, and in another construct, the ksgA gene contained a deletion which resulted in a truncated version of the methylase. When a cell contained one plasmid directing the synthesis of the intact, active methylase and another plasmid encoding the methylase-beta-galactosidase protein, production of the latter product became strongly reduced. Likewise, synthesis of the truncated version of the methylase was diminished when the cell at the same time contained a plasmid producing the complete enzyme. These results were partly substantiated by in vitro experiments with a coupled transcription-translation assay system. By using a recently developed gel electrophoresis system for measuring protein-nucleic acid interactions, a specific binding of the ksgA methylase with its own mRNA could be established. Our results demonstrate that the expression of the ksgA gene can be, at least partly, autogenously controlled at the level of translation.
Knowns and Unknowns of Vitamin B Metabolism in .
Tramonti A, Nardella C, Di Salvo M, Barile A, DAlessio F, de Crecy-Lagard V EcoSal Plus. 2021; 9(2).
PMID: 33787481 PMC: 8995791. DOI: 10.1128/ecosalplus.ESP-0004-2021.
Chiok K, Paul N, Adekanmbi E, Srivastava S, Shah D Microbiol Res. 2018; 216:108-119.
PMID: 30269850 PMC: 6628923. DOI: 10.1016/j.micres.2018.08.009.
Chiok K, Addwebi T, Guard J, Shah D Appl Environ Microbiol. 2013; 79(24):7857-66.
PMID: 24123731 PMC: 3837837. DOI: 10.1128/AEM.03040-13.
Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis.
Boehringer D, OFarrell H, Rife J, Ban N J Biol Chem. 2012; 287(13):10453-10459.
PMID: 22308031 PMC: 3323044. DOI: 10.1074/jbc.M111.318121.
Structural basis for binding of RNA and cofactor by a KsgA methyltransferase.
Tu C, Tropea J, Austin B, Court D, Waugh D, Ji X Structure. 2009; 17(3):374-85.
PMID: 19278652 PMC: 2672589. DOI: 10.1016/j.str.2009.01.010.