Chemotaxis pp 25-49 | Cite as
Prokaryotic Phototaxis
Summary
Microorganisms have various mechanisms at their disposal to react to (changes in) their ambient light climate (i.e., intensity, color, direction, and degree of polarization). Of these, one of the best studied mechanisms is the process of phototaxis. This process can be described as a behavioral migration-response of an organism toward a change in illumination regime. In this chapter we discuss three of these migration responses, based on swimming, swarming, and twitching motility, respectively. Swimming motility has been studied using a wide range of techniques, usually microscopy based. We present a detailed description of the assays used to study phototaxis in liquid cultures of the phototrophic organisms Halobacterium salinarum, Halorhodospira halophila, and Rhodobacter sphaeroides and briefly describe the molecular basis of these responses. Swarming and twitching motility are processes taking place at the interface between a solid phase and a liquid or gas phase. Although assays to study these processes are relatively straightforward, they are accompanied by technical complications, which we describe. Furthermore, we discuss the molecular processes underlying these forms of motility in Rhodocista centenaria and Synechocystis PCC6803. Recently, it has become clear that also chemotrophic organisms contain photoreceptor proteins that allow them to respond to their ambient light climate. Surprisingly, light-modulated motility responses can also be observed in the chemotrophic organisms Escherichia coli and Acinetobacter calcoaceticus. In the light-modulated surface migration not only “che-like” signal transduction reactions may play a role, but in addition processes as modulation of gene expression and even intermediary metabolism.
Key words
Halorhodospira halophila Ectothiorhodospira Halobacterium salinarum Rhodobacter sphaeroides Synechocystis Rhodocista centenaria Rhodospirillum centenum Swimming motility Swarming motility Twitching motility Photoactive yellow protein Sensory rhodopsin Phytochrome BLUF Redox sensingNotes
The authors thank Prof. John L. Spudich valuable comments and Miwa Hara, Mariana Bitrian, Dr. W. Sprenger, and Dr. R. Kort for their contributions to this work. W.D.H. gratefully acknowledges support from NIH grant GM063805 and OCAST grant HR07-135S, and from startup funds provided by Oklahoma State University.
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