Proteomic analyses of the response of cyanobacteria to different stress conditions

Castielli, Ornella; Cerda, Berta de la; Navarro, José A.; Hervás, Manuel; Rosa, Miguel Á. De la

doi:10.1016/j.febslet.2009.03.069

Cited by 62 publications

(30 citation statements)

References 54 publications

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“…Crucially, this "hot-bunking" reduces overall demand for iron, and enables Crocosphaera to do well in oligotrophic environments. Further, recent illustrative examples in which proteomes have been studied in the context of metal ions include studies on metal stress in cyanobacteria [31], in a brown alga [32], and metal-mediated protein dynamics in plants [33]. In addition, recent quantitative "pure" proteomics approaches have also uncovered links with metal ions, for example as shown in Ref.…”

Section: Metalloproteomicsmentioning

confidence: 97%

Protein fractionation and detection for metalloproteomics: challenges and approaches

2012

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At least one third of all proteins are thought to require a metal ion co-factor for their function. Recognition of the importance of metals in biological systems and major advances in analytical instrumentation and technology have led to the emergence of the new research area of metalloproteomics in recent years. Despite this progress, the experimental determination of in-vivo metal cofactors has remained challenging, because this requires elucidation of protein interactions with non-covalently bound metal ions. This critical review highlights current methodological approaches, focusing, in particular, on issues relating to the fractionation and separation of the metalloproteome, including recent experience with metalloproteomics for marine cyanobacteria in our laboratory. Metalloproteomics promises to deliver novel insights into fundamental biological processes in the future, but it is clear that further methodological advances are necessary to exploit the full potential of this emerging research area.

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Section: Metalloproteomicsmentioning

confidence: 97%

Protein fractionation and detection for metalloproteomics: challenges and approaches

2012

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“…Past studies on Synechocystis have revealed that elements such as copper and iron can alter the expression of primary metabolism proteins as well as the expression of general stress proteins such as proteases, chaperones, and sigma factors (54). Recent studies on Synechocystis and Anabaena have demonstrated that iron limitation leads to the expression of the iron stress-induced protein (IsiA) and flavodoxin (IsiB), which act to protect and support the cyanobacterial photosystem (23,55).…”

Section: Discussionmentioning

confidence: 99%

Physiological and Proteomic Responses of Continuous Cultures of Microcystis aeruginosa PCC 7806 to Changes in Iron Bioavailability and Growth Rate

Yeung

D’Agostino

Poljak

et al. 2016

Appl Environ Microbiol

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The hepatotoxin microcystin (MCYST) is produced by a variety of freshwater cyanobacterial species, including Microcystis aeruginosa. Interestingly, MCYST-producing M. aeruginosa strains have been shown to outcompete their nontoxic counterparts under iron-limiting conditions. However, the reasons for this are unclear. Here we examined the proteomic response of M. aeruginosa PCC 7806 continuous cultures under different iron and growth regimes. Iron limitation was correlated with a global reduction in levels of proteins associated with energy metabolism and photosynthesis. These proteomic changes were consistent with physiological observations, including reduced chlorophyll a content and reduced cell size. While levels of MCYST biosynthesis proteins did not fluctuate during the study period, both intra-and extracellular toxin quotas were significantly higher under iron-limiting conditions. Our results support the hypothesis that intracellular MCYST plays a role in protecting the cell against oxidative stress. Further, we propose that extracellular MCYST may act as a signaling molecule, stimulating MCYST production under conditions of iron limitation and enhancing the fitness of bloom populations. IMPORTANCEMicrocystin production in water supply reservoirs is a global public health problem. Understanding the ecophysiology of hepatotoxic cyanobacteria, including their responses to the presence of key micronutrient metals such as iron, is central to managing harmful blooms. To our knowledge, this was the first study to examine proteomic and physiological changes occurring in M. aeruginosa continuous cultures under conditions of iron limitation at different growth rates. C yanobacteria ("blue-green algae") proliferate in warm stratified water bodies rich in nitrogen and phosphorus (1, 2). Cyanobacterial blooms can have a negative impact on the appearance, taste, and odor of water, and their subsequent decay can lead to oxygen depletion and fish kills (3). However, of greatest concern to public health is their production of potent toxins. Microcystis aeruginosa (Kützing) Lemmermann is a common bloom-forming cyanobacterial species that produces hepatotoxic microcystins (MCYSTs) (1). These nonribosomally synthesized peptides inhibit eukaryotic protein phosphatases, leading to liver necrosis in acute doses and hepatocellular carcinoma in chronic low doses (4, 5).There is strong evidence that the production of MCYST is a direct function of cell division (6). It is therefore not surprising that parameters affecting cyanobacterial growth rate (e.g., nutrients, trace metals, temperature, pH, and light) have been correlated with fluctuating MCYST levels in batch culture experiments (7-9).Recent molecular studies suggest that iron (Fe) and nitrogen (N) also play a role in regulating the expression of MCYST biosynthesis (mcy) genes. In M. aeruginosa, for example, the mcy promoter region contains binding sites for the ferric uptake regulator (Fur) and the global nitrogen regulator (NtcA) (10, 11). Despite these genetic clu...

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“…The GroEL proteins are commonly induced by almost all stresses, including heat stress (Apte et al, 1998). Proteomic analyses of Synechocystis PCC6803 exposed to heat, salt or metal stresses similarly indicate the presence of several common proteins, including chaperones and sigma (Sig) factors (Castielli et al, 2009). Protein denaturation occurs in response to almost all abiotic stresses, resulting in accumulation of denatured proteins in the cytosol.…”

Section: The Hsr In Cyanobacteriamentioning

confidence: 99%

Cyanobacterial heat-shock response: role and regulation of molecular chaperones

2014

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Cyanobacteria constitute a morphologically diverse group of oxygenic photoautotrophic microbes which range from unicellular to multicellular, and non-nitrogen-fixing to nitrogen-fixing types. Sustained long-term exposure to changing environmental conditions, during their three billion years of evolution, has presumably led to their adaptation to diverse ecological niches. The ability to maintain protein conformational homeostasis (folding-misfolding-refolding or aggregationdegradation) by molecular chaperones holds the key to the stress adaptability of cyanobacteria. Although cyanobacteria possess several genes encoding DnaK and DnaJ family proteins, these are not the most abundant heat-shock proteins (Hsps), as is the case in other bacteria. Instead, the Hsp60 family of proteins, comprising two phylogenetically conserved proteins, and small Hsps are more abundant during heat stress. The contribution of the Hsp100 (ClpB) family of proteins and of small Hsps in the unicellular cyanobacteria (Synechocystis and Synechococcus) as well as that of Hsp60 proteins in the filamentous cyanobacteria (Anabaena) to thermotolerance has been elucidated. The regulation of chaperone genes by several cis-elements and trans-acting factors has also been well documented. Recent studies have demonstrated novel transcriptional and translational (mRNA secondary structure) regulatory mechanisms in unicellular cyanobacteria. This article provides an insight into the heat-shock response: its organization, and ecophysiological regulation and role of molecular chaperones, in unicellular and filamentous nitrogen-fixing cyanobacterial strains.

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Proteomic analyses of the response of cyanobacteria to different stress conditions

Cited by 62 publications

References 54 publications

Protein fractionation and detection for metalloproteomics: challenges and approaches

Protein fractionation and detection for metalloproteomics: challenges and approaches

Physiological and Proteomic Responses of Continuous Cultures of Microcystis aeruginosa PCC 7806 to Changes in Iron Bioavailability and Growth Rate

Cyanobacterial heat-shock response: role and regulation of molecular chaperones

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