Identification of the ice‐binding face of a plant antifreeze protein

Middleton, Adam J.; Brown, Alan; Davies, Peter L.; Walker, Virginia K.

doi:10.1016/j.febslet.2009.01.035

Cited by 76 publications

(86 citation statements)

References 32 publications

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“…IRI-proteins containing the IRI domains have been previously predicted to form a -roll structure with each of two domain motifs, NxVxxG and NxVxG forming one of the two parallel -sheets that run the length of the protein (Kuiper et al 2001;Tremblay et al 2005;Middleton et al 2009). These Xat, relatively hydrophobic -sheets, also referred to as 'a-side' and 'b-side', had been suggested to serve as ice-binding surfaces, and bind to the prism face of ice crystals.…”

Section: Discussionmentioning

confidence: 98%

Ice recrystallization inhibition proteins of perennial ryegrass enhance freezing tolerance

Zhang

Fei

Arora

et al. 2010

Planta

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Ice recrystallization inhibition (IRI) proteins are thought to play an important role in conferring freezing tolerance in plants. Two genes encoding IRI proteins, LpIRI-a and LpIRI-b, were isolated from a relatively cold-tolerant perennial ryegrass cv. Caddyshack. Amino acid alignments among the IRI proteins revealed the presence of conserved repetitive IRI-domain motifs (NxVxxG/NxVxG) in both proteins. Quantitative reverse transcriptase PCR (qRT-PCR) analysis indicated that LpIRI-a was up-regulated approximately 40-fold while LpIRI-b was up-regulated sevenfold after just 1 h of cold acclimation, and by 7 days of cold acclimation the transcripts had increased 8,000-fold for LpIRI-a and 1,000-fold for LpIRI-b. Overexpression of either LpIRI-a or LpIRI-b gene in Arabidopsis increased survival rates of the seedlings following a freezing test under both cold-acclimated and nonacclimated conditions. For example, without cold acclimation a -4 degrees C treatment reduced the wild type's survival rate to an average of 73%, but resulted in survival rates of 85-100% for four transgenic lines. With cold acclimation, a -12 degrees C treatment reduced the wild type's survival rate to an average of 38.7%, while it resulted in a survival rate of 51-78.5% for transgenic lines. After cold acclimation, transgenic Arabidopsis plants overexpressing either LpIRI-a or LpIRI-b gene exhibited a consistent reduction in freezing-induced ion leakage at -8, -9, and -10 degrees C. Furthermore, the induced expression of the LpIRI-a and LpIRI-b proteins in transgenic E. coli enhanced the freezing tolerance in host cells. Our results suggest that IRI proteins play an important role in freezing tolerance in plants.

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Section: Discussionmentioning

confidence: 98%

Ice recrystallization inhibition proteins of perennial ryegrass enhance freezing tolerance

Zhang

Fei

Arora

et al. 2010

Planta

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“…No data on this from 545 yeast is publically available, although RP titres from yeast systems can be up to several 546 grams per litre culture (Porro et al 2005). E. coli recombinant expression of the LpIBP has 547 been reported up to ~30 mg L -1 (Middleton et al 2009), however, processing to yield a 548 pure product requires several purification steps, including ice-affinity chromatography 549 which would be costly to scale-up, highlighting the value of minimal processing as with 550 CEP from GRAS algal culture. LpIBP exhibits IRI at dilutions as low as 0.055 µM (Yu et 551 al.…”

Section: Discussion 411mentioning

confidence: 99%

Investigating the dynamics of recombinant protein secretion from a microalgal host

Lauersen

Huber

Wichmann

et al. 2015

Journal of Biotechnology

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“…Amino acid residues of the IBS have frequently been identified via mutagenesis studies. 50,66,67 Mutations of amino acids that are important for ice binding result in a large reduction of thermal hysteresis activity. For example, the Thr and Ala residues that are important for ice binding of wfAFP-I are all located on one relatively flat and hydrophobic side of the a-helix.…”

Section: -58mentioning

confidence: 99%

Interaction of ice binding proteins with ice, water and ions

et al. 2016

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Articles you may be interested inExplicit-water theory for the salt-specific effects and Hofmeister series in protein solutions J. Chem. Phys. 144, 215101 (2016) Ice binding proteins (IBPs) are produced by various cold-adapted organisms to protect their body tissues against freeze damage. First discovered in Antarctic fish living in shallow waters, IBPs were later found in insects, microorganisms, and plants. Despite great structural diversity, all IBPs adhere to growing ice crystals, which is essential for their extensive repertoire of biological functions. Some IBPs maintain liquid inclusions within ice or inhibit recrystallization of ice, while other types suppress freezing by blocking further ice growth. In contrast, ice nucleating proteins stimulate ice nucleation just below 0 C. Despite huge commercial interest and major scientific breakthroughs, the precise working mechanism of IBPs has not yet been unraveled. In this review, the authors outline the state-of-the-art in experimental and theoretical IBP research and discuss future scientific challenges. The interaction of IBPs with ice, water and ions is examined, focusing in particular on ice growth inhibition mechanisms.

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Identification of the ice‐binding face of a plant antifreeze protein

Cited by 76 publications

References 32 publications

Ice recrystallization inhibition proteins of perennial ryegrass enhance freezing tolerance

Ice recrystallization inhibition proteins of perennial ryegrass enhance freezing tolerance

Investigating the dynamics of recombinant protein secretion from a microalgal host

Interaction of ice binding proteins with ice, water and ions

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