Chlorosis as a Developmental Program in Cyanobacteria: The Proteomic Fundament for Survival and Awakening

Spät, Philipp; Klotz, Alexander; Rexroth, Sascha; Maček, Boris; Forchhammer, Karl

doi:10.1074/mcp.ra118.000699

Cited by 53 publications

(68 citation statements)

References 81 publications

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“…In contrast to PSII proteins, PSI reaction center proteins PsaA and PsaB were relatively abundant even under N starvation (Figure 2D), which agrees with the proteomic data that PSI proteins are less degraded than PSII proteins with N starvation (Spät et al, 2018). Consistent with these results, Y(ND), which reflects the donor-side limitation of the PSI photochemistry, was remarkably high in N-starved cells, whereas the acceptor-side limitation represented by Y(NA) was negligible (Figures 4B,C).…”

Section: Disorganization Of the Thylakoid Membrane Components By N Stsupporting

confidence: 89%

“…Then we analyzed changes of pigment content based on OD 730 during N starvation and recovery. Previous studies reported that PBSs are subject to rapid degradation in response to N starvation (Collier and Grossman, 1992;Görl et al, 1998;Deschoenmaeker et al, 2014;Spät et al, 2018). In fact, our spectroscopic analysis of intact cells using an integrating sphere demonstrated that N starvation induced a rapid decrease in the absorbance around 626 nm mainly by PBSs ( Figure 1C).…”

Section: Rapid Changes In Pigment Content In Response To N Conditionsmentioning

confidence: 54%

“…Another objective of the active degradation of PBSs may be avoidance of photodamage caused by over reduction of photosynthetic electron carriers due to the low metabolic activity during N starvation (Forchhammer and Schwarz, 2019). The levels of photosystem proteins also decrease under N-starved conditions, with PSII subunits more strongly degraded than PSI subunits (Spät et al, 2018). Thylakoid membranes become almost absent after long-term N starvation, and instead, granules of glycogen and other storage compounds accumulate in the cytosol.…”

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confidence: 99%

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Relationship Between Glycerolipids and Photosynthetic Components During Recovery of Thylakoid Membranes From Nitrogen Starvation-Induced Attenuation in Synechocystis sp. PCC 6803

et al. 2020

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Section: Disorganization Of the Thylakoid Membrane Components By N Stsupporting

confidence: 89%

Section: Rapid Changes In Pigment Content In Response To N Conditionsmentioning

confidence: 54%

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confidence: 99%

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Relationship Between Glycerolipids and Photosynthetic Components During Recovery of Thylakoid Membranes From Nitrogen Starvation-Induced Attenuation in Synechocystis sp. PCC 6803

et al. 2020

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“…This would suggest that monomers are assembled at the TM, and subsequently transported to the PM. A single homolog of MurJ (slr0488), the flippase that translocates peptidoglycan monomers across the PM (Sham et al, 2014), is present in Synechocystis but was not detected in our study or in Spät et al or Liberton et al (Liberton et al, 2016;Spät et al, 2018). Neither was FtsW, responsible for peptidoglycan polymerization in association with PBPs (Taguchi et al, 2019).…”

Section: Assembly Of Cell Wall Components Occurs In Both Membranescontrasting

confidence: 55%

“…Similar scale proteome coverage (2,461 proteins) was recently reported by Spät et al (2018). In their study MS analysis was performed on cells cultured under similar environmental conditions (40 mmol photons m 22 s 21 with air-bubbling at 26°C) to those used here, but which were nitrogen deprived and then harvested 2, 8, 24, and 55 h after resuscitation via addition of nitrate.…”

Section: Extensive Coverage Of the Synechocystis Proteome By Mass Spementioning

confidence: 53%

Proteome Mapping of a Cyanobacterium Reveals Distinct Compartment Organization and Cell-Dispersed Metabolism

et al. 2019

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Cyanobacteria are complex prokaryotes, incorporating a Gram-negative cell wall and internal thylakoid membranes (TMs). However, localization of proteins within cyanobacterial cells is poorly understood. Using subcellular fractionation and quantitative proteomics, we produced an extensive subcellular proteome map of an entire cyanobacterial cell, identifying ;67% of proteins in Synechocystis sp. PCC 6803, ;1000 more than previous studies. Assigned to six specific subcellular regions were 1,712 proteins. Proteins involved in energy conversion localized to TMs. The majority of transporters, with the exception of a TM-localized copper importer, resided in the plasma membrane (PM). Most metabolic enzymes were soluble, although numerous pathways terminated in the TM (notably those involved in peptidoglycan monomer, NADP 1 , heme, lipid, and carotenoid biosynthesis) or PM (specifically, those catalyzing lipopolysaccharide, molybdopterin, FAD, and phylloquinol biosynthesis). We also identified the proteins involved in the TM and PM electron transport chains. The majority of ribosomal proteins and enzymes synthesizing the storage compound polyhydroxybuyrate formed distinct clusters within the data, suggesting similar subcellular distributions to one another, as expected for proteins operating within multicomponent structures. Moreover, heterogeneity within membrane regions was observed, indicating further cellular complexity. Cyanobacterial TM protein localization was conserved in Arabidopsis (Arabidopsis thaliana) chloroplasts, suggesting similar proteome organization in more developed photosynthetic organisms. Successful application of this technique in Synechocystis suggests it could be applied to mapping the proteomes of other cyanobacteria and single-celled organisms. The organization of the cyanobacterial cell revealed here substantially aids our understanding of these environmentally and biotechnologically important organisms.

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Analytical Protocols in Phycobiliproteins Analysis

Nikolić

Minić

Mačvanin

et al. 2020

Pigments From Microalgae Handbook

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The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (10 5 to 10 6 ) and excellent fluorescent quantum yield (0.51 up to 0.98).Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their, bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions, identification by proteomics, phycobiliprotein (chromo)peptides and computational studies of structural and dynamic properties.

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Chlorosis as a Developmental Program in Cyanobacteria: The Proteomic Fundament for Survival and Awakening

Cited by 53 publications

References 81 publications

Relationship Between Glycerolipids and Photosynthetic Components During Recovery of Thylakoid Membranes From Nitrogen Starvation-Induced Attenuation in Synechocystis sp. PCC 6803

Relationship Between Glycerolipids and Photosynthetic Components During Recovery of Thylakoid Membranes From Nitrogen Starvation-Induced Attenuation in Synechocystis sp. PCC 6803

Proteome Mapping of a Cyanobacterium Reveals Distinct Compartment Organization and Cell-Dispersed Metabolism

Analytical Protocols in Phycobiliproteins Analysis

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