title: The RssAB two-component signal transduction system in Serratia marcescens regulates swarming motility and cell envelope architecture in response to exogenous saturated fatty acids.
abstract: Serratia marcescens swarms at 30 degrees C but not at 37 degrees C on a nutrient-rich (LB) agar surface. Mini-Tn5 mutagenesis of S. marcescens CH-1 yielded a mutant (WC100) that swarms not only vigorously at 37 degrees C but also earlier and faster than the parent strain swarms at 30 degrees C. Analysis of this mutant revealed that the transposon was inserted into a gene (rssA) predicted to encode a bacterial two-component signal transduction sensor kinase, upstream of which a potential response regulator gene (rssB) was located. rssA and rssB insertion-deletion mutants were constructed through homologous recombination, and the two mutants exhibited similar swarming phenotypes on LB swarming agar, in which swarming not only occurred at 37 degrees C but also initiated at a lower cell density, on a surface with a higher agar concentration, and more rapidly than the swarming of the parent strain at 30 degrees C. Both mutants also exhibited increased hemolysin activity and altered cell surface topologies compared with the parent CH-1 strain. Temperature and certain saturated fatty acids (SFAs) were found to negatively regulate S. marcescens swarming via the action of RssA-RssB. Analysis of the fatty acid profiles of the parent and the rssA and rssB mutants grown at 30 degrees C or 37 degrees C and under different nutrition conditions revealed a relationship between cellular fatty acid composition and swarming phenotypes. The cellular fatty acid profile was also observed to be affected by RssA and RssB. SFA-dependent inhibition of swarming was also observed in Proteus mirabilis, suggesting that either SFAs per se or the modulation of cellular fatty acid composition and hence homeostasis of membrane fluidity may be a conserved mechanism for regulating swarming motility in gram-negative bacteria.
authors.affiliation: Department of Clinical Laboratory Sciences and Medical Biotechnology, National Taiwan University College of Medicine, Taipei, Taiwan, Republic of China. hclai@ha.mc.ntu.edu.tw
authors.forename: Hsin-Chih
authors.initials: HC
authors.lastname: Lai
authors.forename: Po-Chi
authors.initials: PC
authors.lastname: Soo
authors.forename: Jun-Rong
authors.initials: JR
authors.lastname: Wei
authors.forename: Wen-Ching
authors.initials: WC
authors.lastname: Yi
authors.forename: Shwu-Jen
authors.initials: SJ
authors.lastname: Liaw
authors.forename: Yu-Tze
authors.initials: YT
authors.lastname: Horng
authors.forename: Shi-Ming
authors.initials: SM
authors.lastname: Lin
authors.forename: Shen-Wu
authors.initials: SW
authors.lastname: Ho
authors.forename: Simon
authors.initials: S
authors.lastname: Swift
authors.forename: Paul
authors.initials: P
authors.lastname: Williams
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004251:DNA Transposable Elements / Q000502:physiology; D005227:Fatty Acids / Q000378:metabolism*; D017353:Gene Deletion; D006460:Hemolysin Proteins / Q000378:metabolism; D008124:Locomotion; D008560:Membrane Fluidity / Q000502:physiology; D016254:Mutagenesis, Insertional; D010641:Phenotype; D012706:Serratia marcescens / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D004251:DNA Transposable Elements; D005227:Fatty Acids; D006460:Hemolysin Proteins