Cellular response of Chlorella zofingiensis to exogenous selenium

Pelah, Dan; Cohen, Ephraim

doi:10.1007/s10725-005-3230-6

Cited by 21 publications

(16 citation statements)

References 54 publications

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“…Similar studies have been done with Chlorella zofingiensis with emphasis on heat-stable selenoproteins [30], on metabolism of Se volatile compounds [14], Se effect on Chlorella sp. cultivated on glucose [16], and Se effect on continuous microalgae cultures of Chlorella pyrenoidosa [31] and Chlorella sorokiniana [32].…”

Section: Introductionmentioning

confidence: 70%

Effect of Selenate on Viability and Selenomethionine Accumulation ofChlorella sorokinianaGrown in Batch Culture

Gojkovic

Vílchez

Torronteras

et al. 2014

The Scientific World Journal

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The aim of this work was to study the effect of Se(+VI) on viability, cell morphology, and selenomethionine accumulation of the green alga Chlorella sorokiniana grown in batch cultures. Culture exposed to sublethal Se concentrations of 40 mg·L−1 (212 μM) decreased growth rates for about 25% compared to control. A selenate EC50 value of 45 mg·L−1 (238.2 μM) was determined. Results showed that chlorophyll and carotenoids contents were not affected by Se exposure, while oxygen evolution decreased by half. Ultrastructural studies revealed granular stroma, fingerprint-like appearance of thylakoids which did not compromise cell activity. Unlike control cultures, SDS PAGE electrophoresis of crude extracts from selenate-exposed cell cultures revealed appearance of a protein band identified as 53 kDa Rubisco large subunit of Chlorella sorokiniana, suggesting that selenate affects expression of the corresponding chloroplast gene as this subunit is encoded in the chloroplast DNA. Results revealed that the microalga was able to accumulate up to 140 mg·kg−1 of SeMet in 120 h of cultivation. This paper shows that Chlorella sorokiniana biomass can be enriched in the high value aminoacid SeMet in batch cultures, while keeping photochemical viability and carbon dioxide fixation activity intact, if exposed to suitable sublethal concentrations of Se.

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Section: Introductionmentioning

confidence: 70%

Effect of Selenate on Viability and Selenomethionine Accumulation ofChlorella sorokinianaGrown in Batch Culture

Gojkovic

Vílchez

Torronteras

et al. 2014

The Scientific World Journal

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“…Other workers report upregulation of group 2 proteins or their transcripts after exposure of algae (Chlorella zofingensis) to selenium (Pelah and Cohen 2005) or of bean (Phaseolus vulgaris) to heavy metals such as mercury, cadmium and copper (Zhang et al 2006). In the latter case, the PvSR3 gene did not respond to drought stress or ABA.…”

Section: Ion Binding and Antioxidant Functionmentioning

confidence: 97%

The continuing conundrum of the LEA proteins

Tunnacliffe

Wise

2007

Naturwissenschaften

630

605

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Research into late embryogenesis abundant (LEA) proteins has been ongoing for more than 20 years but, although there is a strong association of LEA proteins with abiotic stress tolerance particularly dehydration and cold stress, for most of that time, their function has been entirely obscure. After their initial discovery in plant seeds, three major groups (numbered 1, 2 and 3) of LEA proteins have been described in a range of different plants and plant tissues. Homologues of groups 1 and 3 proteins have also been found in bacteria and in certain invertebrates. In this review, we present some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlight several possible functions. These include roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as "space fillers" to prevent cellular collapse at low water activities. This multifunctional capacity of the LEA proteins is probably attributable in part to their structural plasticity, as they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. The challenge now facing researchers investigating these enigmatic proteins is to make sense of the various in vitro defined functions in the living cell: Are the LEA proteins truly multi-talented, or are they still just misunderstood?

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“…In PAGE, the electrophoretic mobility of protein depends on the parameters of total charge, molecular weight, configurations and packing (Yamaoka, 1998). The identification of isozymes required use of specific SOD inhibitors as shown for seed plants (Chakrabarty et al, 2007;Kanematsu and Asada, 1989;Martinez et al, 2001;Kim et al, 2004;Sahoo et al, 2001;Seckin et al, 2009), algae (Pelah and Cohen, 2005;Pokora et al, 2003;Zbigniew and Wojciech, 2006), fungi (Belinky et al, 2002;Wang et al, 2005) and oomycetes (Blackman et al, 2005). However, on PGGE, the mobility of proteins was determined only by their molecular sizes irrespective of its ionic charges.…”

Section: Comparison Of Edible Mushroom Sod On Thermostabilitymentioning

confidence: 99%