Isolation and characterization of a novel dehydrin gene from Capsella bursa-pastoris

Fan, Zhengqiu; Wang, X.

doi:10.1134/s0026893306010080

Cited by 8 publications

(4 citation statements)

References 28 publications

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“…Transcriptional regulation of DHN genes in response to stress have been reported for different plant species including Capsicum annuum (Chung et al 2003), Boea crassifolia (Shen et al 2004), Oryza sativa (Lee et al 2005), Capsella bursapastoris (Fan and Wang 2006), Triticum durum (Brini et al 2007), Triticum aestivum L. (Shakirova et al 2009), Populus alba 9 P. tremula var. glandulosa (Bae et al 2009), and Prunus persica L. (Bassett et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library

Ochoa-Alfaro

Rodríguez‐Kessler

Pérez-Morales

et al. 2011

Planta

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Cactus pears are succulent plants of the Cactaceae family adapted to extremely arid, hot and cold environments, making them excellent models for the study of molecular mechanisms underlying abiotic stress tolerance. Herein, we report a directional cDNA library from 12-month-old cladodes of Opuntia streptacantha plants subjected to abiotic stresses. A total of 442 clones were sequenced, representing 329 cactus pear unigenes, classified into eleven functional categories. The most abundant EST (unigen 33) was characterized under abiotic stress. This cDNA of 905 bp encodes a SK(3)-type acidic dehydrin of 248 amino acids. The OpsDHN1 gene contains an intron inserted within the sequence encoding the S-motif. qRT-PCR analysis shows that the OpsDHN1 transcript is specifically accumulated in response to cold stress, and induced by abscisic acid. Over-expression of the OpsDHN1 gene in Arabidopsis thaliana leads to enhanced tolerance to freezing treatment, suggesting that OpsDHN1 participates in freezing stress responsiveness. Generation of the first EST collection for the characterization of cactus pear genes constitutes a useful platform for the understanding of molecular mechanisms of stress tolerance in Opuntia and other CAM plants.

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Section: Introductionmentioning

confidence: 99%

Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library

Ochoa-Alfaro

Rodríguez‐Kessler

Pérez-Morales

et al. 2011

Planta

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“…Experiments, especially on herbaceous plants, are usually carried out by simulating the process of cold acclimation, i.e., by changing the temperature and the duration of the photoperiod under control conditions [ 29 , 47 , 61 ]. Previous studies have been shown changes in herbaceous plant proteins under natural conditions, including common wheat [ 62 ] and alfalfa [ 63 , 64 ]. When analyzing the role of phytohormones in the plant cold acclimation process, the main focus has been on ABA [ 15 , 16 , 19 ], but unfortunately little attention has been paid to IAA [ 23 , 65 , 66 , 67 ] and control of the cold acclimation period with auxin-like compounds.…”

Section: Discussionmentioning

confidence: 99%

The Application of Auxin-like Compounds Promotes Cold Acclimation in the Oilseed Rape Plant

Jankauskienė

Mockevičiūtė

Gavelienė

et al. 2022

Life

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Cold is a major environmental key factor influencing plant growth, development, and productivity. Responses and adaption processes depend on plant physiological and biochemical modifications, first of all via the hormonal system. Indole-3-acetic acid (IAA) plays a critical role in the processes of plant functioning. To assess the influence of the auxin-like compounds 1-[2-chloroethoxycarbonylmethyl]-4-naphthalenesulfonic acid calcium salt (TA-12) and 1-[2-dimethylaminoethoxycarbonylmethyl]naphthalene chloromethylate (TA-14) in the process of cold acclimation, long-term field trials over four years were performed with two rapeseed (Brassica napus L.) plant cultivars with different wintering resistance in temperate-zone countries. In these two rapeseed cultivars, namely ‘Casino’ (less resistant) and ‘Valesca’ (more resistant), investigations were conducted in the terminal buds and root collars. The application of auxin-like compounds revealed a close interlinkage between the composition of dehydrins and the participation of the phytohormone IAA in the adaptation processes. By applying TA-12 and TA-14, the importance of the proteins, especially the composition of the dehydrins, the IAA amount, and the status of the oilseed rape cultivars at the end of the cold acclimation period were confirmed. Following on from this, when introducing oilseed rape cultivars from foreign countries, it may also be of value to assess their suitability for cultivation in temperate-zone countries.

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“…Therefore, it was predicted that the RrMYB113 gene belonged to the R 2 R 3 -MYB [9]. Besides, the random coil is beneficial to the combination of cells with water, and RrMYB113 belongs to the hydrophilic protein, so we presumed that RrMYB113 gene may play a protective role in osmotic stress of plants [27].…”

Section: Discussionmentioning

confidence: 99%

Cloning and Expression Analysis of <i>RrMYB</i>113 Gene Related to Anthocyanin Biosynthesis in <i>Rosa rugose</i>

Zou¹,

Wang²,

Zhao³

et al. 2018

AJPS

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Anthocyanin is one of water-soluble natural pigments widely existing in flowers, fruits, stems, leaves and seeds of plants, and it is the major factor conferring pink or red to the petals of Rosa rugosa. MYB TFs play an important role in the anthocyanin synthesis in plants. This work aimed to clone the MYB gene related to anthocyanin synthesis in the petals of Rosa rugosa, and explore the relationship between them to lay a good foundation for gene engineering improvement of R. rugosa. Based on the transcriptional data, a full-length cDNA sequence of MYB Gene, RrMYB113 (GenBank accession Nos MG720012), was cloned at the first time from the petals of Rosa rugosa "Zi zhi" with RT-PCR and RACE methods. The full-length cDNA is 885 bp with an open reading frame of 654 bp, encoding 216 amino acids. The derived RrMYB113 protein has a molecular weight of 25,297.64 Da, a calculated pI of 9.61, a R 2 R 3 -MYB domain and bHLH binding domain, and it also has the signature motifs ((A/S/G)NDV and KPRPR(T/S)), thus belonging to Sg6 R 2 R 3 -MYB subfamily. In the secondary structure of RrMYB113 protein, there is 37.04% α-helix, 39.81% random coil, 14.81% extended peptide chain, and 8.33% β-corner. There is no transmembrane domain and no signal peptide cleavage site, seventeen Ser phosphorylation sites, fifteen Thr phosphorylation sites, four Tyr phosphorylation sites, and no O-glycosylation sites. The expression of RrMYB113 increased with the color deepening in petals, and it expressed at a higher level in petals than in other tissues of R. rugosa "Zi zhi". These results are meaningful to reveal that RrMYB113 might be an important regulator in anthocyanin biosynthesis and coloration in the petals of R. rugosa.

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Isolation and characterization of a novel dehydrin gene from Capsella bursa-pastoris

Cited by 8 publications

References 28 publications

Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library

Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library

The Application of Auxin-like Compounds Promotes Cold Acclimation in the Oilseed Rape Plant

Cloning and Expression Analysis of <i>RrMYB</i>113 Gene Related to Anthocyanin Biosynthesis in <i>Rosa rugose</i>

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Isolation and characterization of a novel dehydrin gene from Capsella bursa-pastoris

Cited by 8 publications

References 28 publications

Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library

Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library

The Application of Auxin-like Compounds Promotes Cold Acclimation in the Oilseed Rape Plant

Cloning and Expression Analysis of &lt;i&gt;RrMYB&lt;/i&gt;113 Gene Related to Anthocyanin Biosynthesis in &lt;i&gt;Rosa rugose&lt;/i&gt;

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Cloning and Expression Analysis of <i>RrMYB</i>113 Gene Related to Anthocyanin Biosynthesis in <i>Rosa rugose</i>