@article {1444,
	title = {Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {110},
	year = {2013},
	month = {2013 Dec 24},
	pages = {E5069-77},
	abstract = {<p>Bacteria are able to adapt to dramatically different microenvironments, but in many organisms, the signaling pathways, transcriptional programs, and downstream physiological changes involved in adaptation are not well-understood. Here, we discovered that osmotic stress stimulates a signaling network in Mycobacterium tuberculosis regulated by the eukaryotic-like receptor Ser/Thr protein kinase PknD. Expression of the PknD substrate Rv0516c was highly induced by osmotic stress. Furthermore, Rv0516c disruption modified peptidoglycan thickness, enhanced antibiotic resistance, and activated genes in the regulon of the alternative σ-factor SigF. Phosphorylation of Rv0516c regulated the abundance of EspA, a virulence-associated substrate of the type VII ESX-1 secretion system. These findings identify an osmosensory pathway orchestrated by PknD, Rv0516c, and SigF that enables adaptation to osmotic stress through cell wall remodeling and virulence factor production. Given the widespread occurrence of eukaryotic-like Ser/Thr protein kinases in bacteria, these proteins may play a broad role in bacterial osmosensing.</p>},
	keywords = {Adaptation, Biological, Blotting, Western, Gene Expression Regulation, Bacterial, Green Fluorescent Proteins, Microarray Analysis, Mycobacterium tuberculosis, Osmolar Concentration, Osmotic Pressure, Phosphorylation, Protein Kinases, Signal Transduction},
	issn = {1091-6490},
	doi = {10.1073/pnas.1321205110},
	author = {Hatzios, Stavroula K and Baer, Christina E and Rustad, Tige R and Siegrist, M Sloan and Pang, Jennifer M and Ortega, Corrie and Alber, Tom and Grundner, Christoph and Sherman, David R and Bertozzi, Carolyn R}
}
@article {440,
	title = {Novel regulatory cascades controlling expression of nitrogen-fixation genes in Geobacter sulfurreducens.},
	journal = {Nucleic Acids Res},
	volume = {38},
	year = {2010},
	month = {2010 Nov},
	pages = {7485-99},
	abstract = {Geobacter species often play an important role in bioremediation of environments contaminated with metals or organics and show promise for harvesting electricity from waste organic matter in microbial fuel cells. The ability of Geobacter species to fix atmospheric nitrogen is an important metabolic feature for these applications. We identified novel regulatory cascades controlling nitrogen-fixation gene expression in Geobacter sulfurreducens. Unlike the regulatory mechanisms known in other nitrogen-fixing microorganisms, nitrogen-fixation gene regulation in G. sulfurreducens is controlled by two two-component His-Asp phosphorelay systems. One of these systems appears to be the master regulatory system that activates transcription of the majority of nitrogen-fixation genes and represses a gene encoding glutamate dehydrogenase during nitrogen fixation. The other system whose expression is directly activated by the master regulatory system appears to control by antitermination the expression of a subset of the nitrogen-fixation genes whose transcription is activated by the master regulatory system and whose promoter contains transcription termination signals. This study provides a new paradigm for nitrogen-fixation gene regulation.},
	keywords = {Bacterial Proteins, Binding Sites, DNA-Binding Proteins, Gene Expression Regulation, Bacterial, Geobacter, Nitrogen Fixation, Promoter Regions, Genetic, Protein Kinases, RNA-Binding Proteins, Transcription, Genetic},
	issn = {1362-4962},
	doi = {10.1093/nar/gkq652},
	author = {Ueki, Toshiyuki and Lovley, Derek R}
}
@article {390,
	title = {Altered phosphorylation/inactivation of a novel pyruvate dehydrogenase in adult Ascaris suum muscle.},
	journal = {Mol Biochem Parasitol},
	volume = {90},
	year = {1997},
	month = {1997 Dec 1},
	pages = {323-6},
	keywords = {Animals, Ascaris suum, Cattle, Kidney, Muscles, Phosphorylation, Protein Kinases, Protein-Serine-Threonine Kinases, Pyruvate Dehydrogenase (Lipoamide), Pyruvate Dehydrogenase Complex},
	issn = {0166-6851},
	author = {Klingbeil, M M and Walker, D J and Huang, Y J and Komuniecki, R}
}
