Enhanced uptake of potassium or glycine betaine or export of cyclic-di-AMP restores osmoresistance in a high cyclic-di-AMP Lactococcus lactis mutant

• Published in: PLoS genetics Vol. 14; no. 8; p. e1007574
• Main Authors: Pham, Huong Thi, Nhiep, Nguyen Thi Hanh, Vu, Thu Ngoc Minh, Huynh, TuAnh Ngoc, Zhu, Yan, Huynh, Anh Le Diep, Chakrabortti, Alolika, Marcellin, Esteban, Lo, Raquel, Howard, Christopher B, Bansal, Nidhi, Woodward, Joshua J, Liang, Zhao-Xun, Turner, Mark S
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 03.08.2018; Public Library of Science (PLoS)
• Subjects: ABC transporters; Adenosine Monophosphate; AMP; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - physiology; Betaine - metabolism; Bioengineering; Biology and Life Sciences; Cell division; Cyclic AMP - metabolism; E coli; Enzymes; Food; Funding; Gene Expression Regulation, Bacterial; Glycine; Glycine betaine; Gram-positive bacteria; Intracellular; Lactococcus; Lactococcus lactis - genetics; Lactococcus lactis - physiology; Medicine and Health Sciences; Multidrug resistance; Mutation; Nanotechnology; Operon; Osmolar Concentration; Osmolarity; Osmoprotectants; Osmoregulation; Phosphodiesterase; Physical Sciences; Physiological aspects; Potassium; Potassium (Nutrient); Potassium - metabolism; Proteins; Research and Analysis Methods; Second Messenger Systems; Sensors; Streptococcus infections; Supervision; Transcription; Turgor; Water stress; Singapore; Queensland Australia; Australia; United States > US

The broadly conserved bacterial signalling molecule cyclic-di-adenosine monophosphate (c-di-AMP) controls osmoresistance via its regulation of potassium (K+) and compatible solute uptake. High levels of c-di-AMP resulting from inactivation of c-di-AMP phosphodiesterase activity leads to poor growth...