Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.)

Simpson, Deborah J.; Smallwood, Maggie; Twigg, Sarah; Doucet, Charlotte J.; Ross, Joe; Bowles, Dianna J.

doi:10.1016/j.cryobiol.2005.06.005

Cited by 25 publications

(22 citation statements)

References 9 publications

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“…Two previous reports suggested that dehydrins also have the ability to shape ice crystals and prevent their growth at moderate subzero temperatures (Wisniewski et al, 1999;Simpson et al, 2005). This activity was suggested to come from the dehydrin present in peach (Prunus persica) bark (PCA60; Wisniewski et al, 1999) and from a partially purified and characterized Forsythia suspensa protein that may contain K-segments (Simpson et al, 2005).…”

Section: Potential Afp Activity Of Dehydrinsmentioning

confidence: 99%

“…In vitro, dehydrins have been shown to protect enzymes from freeze-thaw damage (Lin and Thomashow, 1992;Kazuoka and Oeda, 1994;Momma et al, 2003;Goyal et al, 2005;Hughes and Graether, 2011) and heat denaturation (Kovacs et al, 2008), interact with and protect membranes from cold and dehydrative stresses (Rahman et al, 2010;, and bind water (Tompa et al, 2006), ions (Alsheikh et al, 2003), and nucleic acids (Hara et al, 2009). Dehydrins have also been suggested to prevent the growth of ice crystals by functioning in a manner similar to antifreeze proteins (AFPs; Wisniewski et al, 1999;Simpson et al, 2005).…”

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confidence: 99%

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The Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins

et al. 2013

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Dehydrins protect plant proteins and membranes from damage during drought and cold. Vitis riparia K 2 is a 48-residue protein that can protect lactate dehydrogenase from freeze-thaw damage by preventing the aggregation and denaturation of the enzyme. To further elucidate its mechanism, we used a series of V. riparia K 2 concatemers (K 4 , K 6 , K 8 , and K 10 ) and natural dehydrins (V. riparia YSK 2 , 60 kilodalton peach dehydrin [PCA60], barley dehydrin5 [Dhn5], Thellungiella salsuginea dehydrin2 , and Opuntia streptacantha dehydrin1 ) to test the effect of the number of K-segments and dehydrin size on their ability to protect lactate dehydrogenase from freeze-thaw damage. The results show that the larger the hydrodynamic radius of the dehydrin, the more effective the cryoprotection. A similar trend is observed with polyethylene glycol, which would suggest that the protection is simply a nonspecific volume exclusion effect that can be manifested by any protein. However, structured proteins of a similar range of sizes did not show the same pattern and level of cryoprotection. Our results suggest that with respect to enzyme protection, dehydrins function primarily as molecular shields and that their intrinsic disorder is required for them to be an effective cryoprotectant. Lastly, we show that the cryoprotection by a dehydrin is not due to any antifreeze proteinlike activity, as has been reported previously.

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Section: Potential Afp Activity Of Dehydrinsmentioning

confidence: 99%

mentioning

confidence: 99%

The Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins

et al. 2013

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“…For bark and leaves of Forsythia suspensa, also cold-acclimated under natural conditions, for example, the antifreeze activity was observed in a single protein with apparent molecular mass of 20 kDa (SIMPSON et al, 2005). Kontogiorgos et al (2006) reported that apoplastic extract of the cold-acclimated winter wheat grass contained only heat-stable RI protein with a molecular weight below 40 kDa.…”

Section: Resultsmentioning

confidence: 99%

“…Since Griffith et al (1992) described, in a pioneering way, the presence of AFPs in winter rye leaves (Secale cereale), which were later studied by Hon et al (1994), Antikainen and Griffith (1997) and Lim et al (2013), the presence of AFPs with different characteristics have been detected in wheat (Triticum aestivum) (ANTIKAINEN; GRIFFITH, 1997;ZHANG et al, 2007), carrots (Daucus carota) (SMALLWOOD et al, 1999;WANG et al, 2002;ZHANG et al, 2004;GOMEZ GALINDO et al, 2005;DING et al, 2014), ryegrass (Lolium perenne) (SIDEBOTTOM et al, 2000;PUDNEY et al, 2003;MIDDLETON et al, 2012), Solanum tuberosum (URRUTIA et al, 1992), Solanum dulcamara (URRUTIA et al, 1992;DUMAN, 2002), Forsythia suspensa (SIMPSON et al, 2005), Picea abis and Picea pungens (JARZABEK et al, 2009), among many others.…”

Section: Introductionmentioning

confidence: 99%

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Antifreeze proteins in naturally cold acclimated leaves of Drimys angustifolia, Senecio icoglossus, and Eucalyptus ssp.

Provesi

Valentim-Neto

Arisi

et al. 2016

Braz. J. Food Technol.

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Antifreeze proteins in naturally cold acclimated leaves of Drimys angustifolia,Senecio icoglossus, and Eucalyptus ssp. Avaliação de proteínas anticongelantes em folhas de Drimys angustifolia, Senecio icoglossus e Eucalyptus ssp. naturalmente aclimatadas ao frio SummaryAntifreeze proteins (AFPs) present in plants may inhibit ice recrystallization even at low concentrations, and show potential application to many frozen foods. This study evaluated the presence of antifreeze proteins in naturally cold acclimated and non-acclimated leaves of Drimys angustifolia, Senecio icoglossus and Eucalyptus ssp. No proteins were detected in apoplastic extracts of Eucalyptus ssp. Extracts of cold acclimated and non-acclimated S. icoglossus showed protein concentrations of 42.89 and 17.76 µg mL -1 , both with bands between 25 and 37 kDa in the SDS-PAGE. However, they did not inhibit recrystallization. The extract of cold acclimated D. angustifolia contained a protein concentration of 95.17 µg mL -1 , almost five times higher than the extract of non-acclimated D. angustifolia. In the extract of cold acclimated D. angustifolia, there was presence of ice recrystallization inhibitors. This extract showed a protein band just below 37 kDa and another more intense band between 20 and 25 kDa. It is the first time that the presence of antifreeze proteins in this species is being described. Keywords: Antifreeze protein; Drimys angustifolia; Senecio icoglossus; Eucalyptus; Natural cold acclimation; Recrystallization inhibition. ResumoProteínas anticongelantes (PACs) de plantas podem inibir a recristalização do gelo mesmo em baixas concentrações, tendo potencial para aplicação em diversos alimentos congelados. Este trabalho avaliou a presença de proteínas anticongelantes em folhas naturalmente aclimatadas ao frio e folhas não aclimatadas de Drimys angustifolia, Senecio icoglossus e Eucalyptus ssp. Não foram detectadas proteínas nos extratos de Eucalyptus ssp. Os extratos de folhas aclimatadas e não aclimatadas de S. icoglossus apresentaram concentrações de proteína de 42,89 e 17,76 µg mL -1 , respectivamente, verificando-se, em ambos os extratos, bandas entre 25 e 37 kDa no SDS-PAGE. Contudo, esses extratos não apresentaram atividade de inibição da recristalização. O extrato de folhas de D. angustifolia aclimatadas ao frio apresentou concentração de proteína de 95,17 µg mL -1 , cinco vezes maior do que extrato não aclimatado dessa espécie. Observou-se que o extrato aclimatado de D. angustifolia apresentou atividade de inibição da recristalização. Esse extrato apresentou uma banda logo abaixo de 37 kDa e outra mais intensa, entre 20 e 25 kDa no SDS-PAGE. É a primeira vez que a presença de proteínas anticongelantes, nessa espécie, é descrita. Palavras

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Nitric oxide-cold stress signalling cross-talk, evolution of a novel regulatory mechanism

2013

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Plants enhance their cold stress tolerance by cold acclimation, a process which results in vast reprogramming of transcriptome, proteome and metabolome. Evidence suggests nitric oxide (NO) production during cold stress which regulates genes (especially the C-repeat binding factor (CBF) cold stress signalling pathway), diverse proteins including transcription factors (TFs) and phosphosphingolipids. About 59% (redox), 50% (defence/stress) and 30% (signalling) cold responsive proteins are modulated by NO-based post translational modifications (PTMs) namely S-nitrosylation, tyrosine nitration and S-glutathionylation, suggesting a cross-talk between NO and cold. Analysis of cold stress responsive deep proteome in apoplast, mitochondria, chloroplast and nucleus suggested continuation of this cross-talk in sub-cellular systems. Modulation of cold responsive proteins by these PTMs right from cytoskeletal elements in plasma membrane to TFs in nucleus suggests a novel regulation of cold stress signalling. NO-mediated altered protein transport in nucleus seems an important stress regulatory mechanism. This review addresses the NO and cold stress signalling cross-talk to present the overview of this novel regulatory mechanism.

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Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.)

Cited by 25 publications

References 9 publications

The Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins

The Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins

Antifreeze proteins in naturally cold acclimated leaves of Drimys angustifolia, Senecio icoglossus, and Eucalyptus ssp.

Nitric oxide-cold stress signalling cross-talk, evolution of a novel regulatory mechanism

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