Abstract

CONTENT ALERTS Receive: RSS Feeds, eTOCs, free email alerts (when new articles cite this article), more» Information about commercial reprint orders: http://jb.asm.org/site/misc/reprints.xhtml To subscribe to to another ASM Journal go to: http://journals.asm.org/site/subscriptions/ JOURNAL OF BACTERIOLOGY, Apr. 1992, P. 2053-2058 Vol. 174, No. 7 0021-9193/92/072053-06$02.00/0 Copyright © 1992, American Society for Microbiology Is Cross Regulation by Phosphorylation of Two-Component Response Regulator Proteins Important in Bacteria?t BARRY L. WANNER Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907 INTRODUCTION A large family of structurally and functionally similar two-component regulatory systems exists in bacteria. In general, these systems consist of pairs of partner proteins called sensors and response regulators. Sensors are important in signal transduction and share sequence similarities at the protein level. They probably all act as histidine protein kinases that can phosphorylate themselves and as phosphotransferases that can interact with and phosphorylate partner regulators, which also share sequence similarities among themselves. Sensors detect extracellular (environmental) or intracellular stimuli and transfer signals to response regulators by phosphorylation, a process that in turn controls the activity of regulators of chemotaxis and gene expression. In addition, response regulators may receive input signals from different regulatory systems, which in at least one