nblS, a Gene Involved in Controlling Photosynthesis-Related Gene Expression during High Light and Nutrient Stress inSynechococcus elongatusPCC 7942
- 1 May 2002
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 184 (9) , 2481-2490
- https://doi.org/10.1128/jb.184.9.2481-2490.2002
Abstract
The HliA protein of the cyanobacteriumSynechococcus elongatusPCC 7942 is a small, thylakoid-associated protein that appears to play a role in photoprotection; its transcript rapidly accumulates in response to high-intensity light (HL) and thehligene family is required for survival of cells in high light. In order to discover regulatory factors involved in HL acclimation in cyanobacteria, a screen was performed for chemically generated mutants unable to properly control expression of thehliAgene in response to HL. One such mutant was identified, and complementation analysis led to the identification of the affected gene, designatednblS. Based on its deduced protein sequence, NblS appears to be a membrane-bound, PAS-domain-bearing, sensor histidine kinase of two-component regulatory systems in bacteria. ThenblSmutant was unable to properly control light intensity-mediated expression of several other photosynthesis-related genes, including all threepsbAgenes and thecpcBAgenes. The mutant was also unable to control expression of thehliAandpsbAgenes in response to low-intensity blue/UV-A light, a response that may be related to the HL-mediated regulation of the genes. Additionally, in response to nutrient deprivation, thenblSmutant was unable to properly control accumulation of thenblAtranscript and associated degradation of the light-harvesting phycobilisomes. ThenblSmutant dies more rapidly than wild-type cells following exposure to HL or nutrient deprivation, likely due to its inability to properly acclimate to these stress conditions. Thus, the NblS protein is involved in the control of a number of processes critical for altering the photosynthetic apparatus in response to both HL and nutrient stress conditions.Keywords
This publication has 63 references indexed in Scilit:
- The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteinsFEMS Microbiology Letters, 1999
- PHOTOPROTECTION REVISITED:Genetic and Molecular ApproachesAnnual Review of Plant Biology, 1999
- Sequence Evidence for Strong Conservation of the Photoactive Yellow Proteins from the Halophilic Phototrophic Bacteria Chromatium salexigens and Rhodospirillum salexigensBiochemistry, 1996
- LIGHT-HARVESTING COMPLEXES IN OXYGENIC PHOTOSYNTHESIS: Diversity, Control, and EvolutionAnnual Review of Genetics, 1995
- The dspA gene product of the cyanobacterium Synechocystis sp. strain PCC 6803 influences sensitivity to chemically different growth inhibitors and has amino acid similarity to histidine protein kinasesMicrobiology, 1995
- COMMUNICATION MODULES IN BACTERIAL SIGNALING PROTEINSAnnual Review of Genetics, 1992
- Photoprotection and Other Responses of Plants to High Light StressAnnual Review of Plant Biology, 1992
- Physiological and Molecular Studies of Light-Regulated Nuclear Genes in Higher PlantsAnnual Review of Plant Biology, 1991
- Photoregulation of the Composition, Function, and Structure of Thylakoid MembranesAnnual Review of Plant Physiology, 1986
- Mutagenesis by nitrosoguanidine, ethyl methanesulfonate, and mutator gene mutH in continuous cultures of Escherichia coliMutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 1975