Peptide Mapping and Assessment of Cryoprotective Activity of 26/27-kDa Dehydrin from Soybean Seeds

Momma, Mitsuru; Kaneko, Shigeo; Haraguchi, Kazutomo; Matsukura, Ushio

doi:10.1271/bbb.67.1832

Cited by 38 publications

(28 citation statements)

References 6 publications

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“…Using NMR chemical shifts and relaxation data (Hughes and Graether, 2011), we have shown that in solution the K-segment is very weakly a-helical and flexible, while the f-segment has no secondary structure preference whatsoever and is highly flexible. Despite its small size (48 residues), the V. riparia K 2 was very effective at protecting lactate dehydrogenase (LDH) from freeze-thaw damage (Hughes and Graether, 2011), a model enzyme used in many cryoprotective studies (Lin and Thomashow, 1992;Kazuoka and Oeda, 1994;Momma et al, 2003;Goyal et al, 2005). Although these two proteins do not bind to one another (Hughes and Graether, 2011), we showed that K 2 prevents LDH from denaturing and aggregating.…”

mentioning

confidence: 86%

“…Numerous studies have reported on the ability of dehydrins to protect LDH from losing activity after being frozen and thawed (Lin and Thomashow, 1992;Kazuoka and Oeda, 1994;Houde et al, 1995;Hara et al, 2001;Momma et al, 2003;Goyal et al, 2005). Previously, we had shown that the 48-residue K 2 protein is able to protect the enzyme from freeze-thaw damage despite its small size (Hughes and Graether, 2011).…”

Section: Enzymatic Cryoprotectionmentioning

confidence: 98%

“…Dehydrins are thought to be involved in dehydration protection, since their transcription and translation are increased during dehydration, and a correlation exists between drought tolerance and the amount of dehydrin present. 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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confidence: 86%

Section: Enzymatic Cryoprotectionmentioning

confidence: 98%

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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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“…The KS-type dehydrin, Glyma17g24193 contains ABRE sites (and no CRT/DRE), and is up-regulated by exogenous ABA treatment [33]. Mat9 (Glyma09g31740) and Mat1 (Glyma07g10030) are dehydrins, which are primarily expressed in seeds and contain many potential ABRE elements [58,59]. Maruyama et al [17] showed a high frequency of ABREs in the promoters of cold inducible genes in soybean.…”

Section: Soybean Dehydrins Are Not Directly Regulated By the Cbf Pathmentioning

confidence: 99%

Functionality of soybean CBF/DREB1 transcription factors

Yamasaki

Randall

2016

Plant Science

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Soybean (Glycine max) is considered to be cold intolerant and is not able to significantly acclimate to cold/freezing stress. In most cold tolerant plants, the Crepeat/DRE Binding Factors (CBF/DREBs) are critical contributors to successful cold-responses; rapidly increasing following cold treatment and regulating the induction of many cold responsive genes. In soybean vegetative tissue, we found strong, transient accumulation of CBF transcripts in response to cold stress; however, the soybean transcripts of typical cold responsive genes (homologues to Arabidopsis genes such as dehydrins, ADH1, RAP2.1, and LEA14) were not significantly altered.Soybean CBFs were found to be functional, as when expressed constitutively in Arabidopsis they increased the levels of AtCOR47 and AtRD29a transcripts and increased freezing tolerance as measured by a decrease in leaf freezing damage and ion leakage. Furthermore the constitutive expression of GmDREB1A;2 and GmDREB1B;1 in Arabidopsis led to stronger up-regulation of downstream genes and more freezing tolerance than GmDREB1A;1, the gene whose transcript is the major contributor to total CBF/DREB1 transcripts in soybean. The inability for the soybean CBFs to significantly up regulate the soybean genes that contribute to cold tolerance is consistent with poor acclimation capability and the cold intolerance of soybean.

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“…A broad protein stabilization function and antiaggregation activity have been shown for a group 3 LEA protein from Aphelenchus avenae (Chakrabortee et al, 2007). Cryoprotective activity on lactate dehydrogenase has been demonstrated for two DHN-type proteins (Momma et al, 2003), and a similar effect was also shown for PCA60, a 60-kD protein from winter bark tissues of peach (Prunus persica; Wisniewskia et al, 1999). All of these points might be taken to suggest that ERD10 and ERD14 exploit their structural disorder in fulfilling protective functions by chaperone activity, membrane binding, or both.…”

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confidence: 99%

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

et al. 2008

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ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to abiotic environmental stresses, such as high salinity, drought, and low temperature, in Arabidopsis (Arabidopsis thaliana). Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remains poorly understood. Here, detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperones in vitro. ERD10 and ERD14 are able to prevent the heat-induced aggregation and/or inactivation of various substrates, such as lysozyme, alcohol dehydrogenase, firefly luciferase, and citrate synthase. It is also demonstrated that ERD10 and ERD14 bind to acidic phospholipid vesicles without significantly affecting membrane fluidity. Membrane binding is strongly influenced by ionic strength. Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces. We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses.

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Peptide Mapping and Assessment of Cryoprotective Activity of 26/27-kDa Dehydrin from Soybean Seeds

Cited by 38 publications

References 6 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

Functionality of soybean CBF/DREB1 transcription factors

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

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