Many photosynthetic autotrophs have evolved responses that adjust their metabolism to limitations in nutrient availability. Here we report a detailed characterization of the remodeling of photosynthesis upon sulfur starvation under heterotrophy and photo-autotrophy in the green alga (). Photosynthetic inactivation under low light and darkness is achieved through specific degradation of Rubisco and cytochrome and occurs only in the presence of reduced carbon in the medium. The process is likely regulated by nitric oxide (NO), which is produced 24 h after the onset of starvation, as detected with NO-sensitive fluorescence probes visualized by fluorescence microscopy. We provide pharmacological evidence that intracellular NO levels govern this degradation pathway: the addition of a NO scavenger decreases the rate of cytochrome and Rubisco degradation, whereas NO donors accelerate the degradation. Based on our analysis of the relative contribution of the different NO synthesis pathways, we conclude that the NO-dependent nitrate reductase-independent pathway is crucial for NO production under sulfur starvation. Our data argue for an active role for NO in the remodeling of thylakoid protein complexes upon sulfur starvation.
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http://dx.doi.org/10.1104/pp.18.01164 | DOI Listing |
J Biol Chem
December 2024
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA. Electronic address:
Glutathione (GSH) is an abundant thiol-containing tripeptide that functions in redox homeostasis, protein folding, and iron metabolism. In Saccharomyces cerevisiae, GSH depletion leads to increased sensitivity to oxidants and other toxic compounds, disruption of Fe-S cluster biogenesis, and eventually cell death. GSH pools are supplied by intracellular biosynthesis and GSH import from the extracellular environment.
View Article and Find Full Text PDFmSystems
December 2024
Department of Bioengineering, University of California, San Diego, California, USA.
Unlabelled: The composition of bacterial transcriptomes is determined by the transcriptional regulatory network (TRN). The TRN regulates the transition from one physiological state to another. Here, we use independent component analysis to monitor the composition of the transcriptome during the transition from the exponential growth phase to the stationary phase.
View Article and Find Full Text PDFWater Res
November 2024
Guangdong Provincial Engineering Research Center for Urban Water Recycling and Environmental Safety, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, Guangdong 518055, PR China; Key Laboratory of Microorganism Application and Risk Control, Ministry of Ecology and Environment, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, Guangdong 518055, PR China; Shenzhen Key Laboratory of Ecological Remediation and Carbon Sequestration, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, Guangdong 518055, PR China; Tsinghua University-Kunming Joint Research Center for Dianchi Plateau Lake, Tsinghua University, Beijing 100084, PR China. Electronic address:
Proc Natl Acad Sci U S A
November 2024
Department of Chemistry, University of Massachusetts, Boston, MA 02125.
Sulfur is an essential element for life. Bacteria can obtain sulfur from inorganic sulfate; but in the sulfur starvation-induced response, employ two-component flavin-dependent monooxygenases (TC-FMOs) from the and operons to assimilate sulfur from environmental compounds including alkanesulfonates and dialkylsulfones. Here, we report binding studies of oxidized FMN to enzymes involved within the enzymatic pathway responsible for converting dimethylsulfone (DMSO) to sulfite.
View Article and Find Full Text PDFbioRxiv
October 2024
Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA.
Under conditions of oxidative stress or iron starvation, iron-sulfur cluster biogenesis in is initiated by the cysteine desulfurase, SufS, via the SUF pathway. SufS is a type II cysteine desulfurase that catalyzes the PLP-dependent breakage of an L-cysteine C-S bond to generate L-alanine and a covalent active site persulfide as products. The persulfide is transferred from SufS to SufE and then to the SufBCD complex, which utilizes it in iron-sulfur cluster biogenesis.
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