Cloning, expression and characterization of novel avenin-like genes in wheat and related species

Peng, Chen; Wang, Changdong; Li, Kexiu; Chang, Junli; Wang, Yue-Sheng; Yang, Guangxiao; Shewry, Peter R.; He, Guoqing

doi:10.1016/j.jcs.2008.04.002

Cited by 23 publications

(38 citation statements)

References 24 publications

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“…The supernatant was filtered through a 0.45-m membrane and purified by affinity chromatography using a nickel-nitrilotriacetic acid column (Ni-NTA agarose; Roche). The protein was renatured through step dialysis at 4°C for 12 h. The primary polyclonal antibody was produced via the immunization of a New Zealand rabbit with AgRPL44 protein (31).…”

Section: Methodsmentioning

confidence: 99%

Abiotic Stress Resistance, a Novel Moonlighting Function of Ribosomal Protein RPL44 in the Halophilic Fungus Aspergillus glaucus

Liu

Xie

et al. 2014

Appl Environ Microbiol

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bRibosomal proteins are highly conserved components of basal cellular organelles, primarily involved in the translation of mRNA leading to protein synthesis. However, certain ribosomal proteins moonlight in the development and differentiation of organisms. In this study, the ribosomal protein L44 (RPL44), associated with salt resistance, was screened from the halophilic fungus Aspergillus glaucus (AgRPL44), and its activity was investigated in Saccharomyces cerevisiae and Nicotiana tabacum. Sequence alignment revealed that AgRPL44 is one of the proteins of the large ribosomal subunit 60S. Expression of AgRPL44 was upregulated via treatment with salt, sorbitol, or heavy metals to demonstrate its response to osmotic stress. A homologous sequence from the model fungus Magnaporthe oryzae, MoRPL44, was cloned and compared with AgRPL44 in a yeast expression system. The results indicated that yeast cells with overexpressed AgRPL44 were more resistant to salt, drought, and heavy metals than were yeast cells expressing MoRPL44 at a similar level of stress. When AgRPL44 was introduced into M. oryzae, the transformants displayed obviously enhanced tolerance to salt and drought, indicating the potential value of AgRPL44 for genetic applications. To verify the value of its application in plants, tobacco was transformed with AgRPL44, and the results were similar. Taken together, we conclude that AgRPL44 supports abiotic stress resistance and may have value for genetic application.

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Section: Methodsmentioning

confidence: 99%

Abiotic Stress Resistance, a Novel Moonlighting Function of Ribosomal Protein RPL44 in the Halophilic Fungus Aspergillus glaucus

Liu

Xie

et al. 2014

Appl Environ Microbiol

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“…The open reading frame (ORF) of farinin genes in B. distachyon accessions were amplified with two pairs of AS-PCR primers designed according to previous reports (Kan et al 2006;Chen et al 2008). To amplify the promoter region, a pair of primers were designed according to the published complete coding sequences (CDS) of farinin genes (JN622144) in the NCBI database.…”

Section: Plant Materialsmentioning

confidence: 99%

“…Based on amplified distinct identical and divergent clone sequences, ALPs were further classified into a1, a2, and a3 and b1, b2, and b3 types (Kan et al 2006). ALP b-type genes were then reported from various Aegilops species that exhibited close evolutionary relationships with wheat (Chen et al 2008). The a-type ALPs were similar to LMW gliadins and were disengaged from the gluten polymer through S-S bonds (Clarke et al 2003;de Gregorio et al 2009).…”

Section: Introductionmentioning

confidence: 99%

“…Because farinins do not show high similarity to gliadins compared with ALPs, the term Bfarinin^was proposed to apply to all ALPs found in wheat and Aegilops as a novel nomenclature (Kasarda et al 2013. Apart from these functional properties, farinin genes from Triticum and its related species can be used to investigate evolutionary relationships within Triticeae tribes (Kan et al 2006;Chen et al 2008).…”

Section: Introductionmentioning

confidence: 99%

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Molecular characterization and evolutionary origins of farinin genes in Brachypodium distachyon L.

Subburaj

Luo

et al. 2015

J Appl Genetics

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Farinins are one of the oldest members of the gluten family in wheat and Aegilops species, and they influence dough properties. Here, we performed the first detailed molecular genetic study on farinin genes in Brachypodium distachyon L., the model species for Triticum aestivum. A total of 51 b-type farinin genes were cloned and characterized, including 27 functional and 24 non-functional pseudogenes from 14 different B. distachyon accessions. All genes were highly similar to those previously reported from wheat and Aegilops species. The identification of deduced amino acid sequences showed that b-type farinins across Triticeae genomes could be classified as b1-, b2-, b3-, and b4-type farinins; however, B. distachyon had only b3- and b4-type farinins. Real-time quantitative reverse transcription polymerase chain reaction (qRT-PCR) revealed that farinin genes are transcribed into mRNA in B. distachyon at much lower levels than in Triticeae, despite the presence of cis-acting elements in promoter regions. Phylogenetic analysis suggested that Brachypodium farinins may have closer relationships with common wheat and further confirmed four different types of b-type farinins in Triticeae and Brachypodium genomes, corresponding to b1, b2, b3 (group 1), and b4 (group 2). A putative evolutionary origin model of farinin genes in Brachypodium, Triticum, and the related species suggests that all b-type farinins diverged from their common ancestor ~3.2 million years ago (MYA). The b3 and b4 types could be considered older in the farinin family. The results explain the loss of b1- and b2-type farinin alleles in Brachypodium.

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“…The fragments were recovered by using a gel extraction kit (TaKaRa, Dalian, China) and cloned into the pMD18-T vector (TaKaRa, Dalian, China). The vector was then transformed into Escherichia coli (DH5a) competent cells as described by Chen et al (2008). PCR and restriction enzyme digestion were carried out to identify the positive clones.…”

Section: Plant Materialsmentioning

confidence: 99%

Cloning and characterization of novel low molecular weight glutenin subunit genes from two Aegilops species with the C and D genomes

Chen

Zhou

et al. 2010

Genet Resour Crop Evol

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Four novel low molecular weight glutenin subunit genes (designated as AmLMWm1, AcLMWm1, AcLMWm2 and AcLMWm3) were isolated and characterized from the genomic DNA of two Aegilops accessions, AmLMWm1 from Aegilops markgrafii (Greuter) K.Hammer (2n = 2x = 14, CC), AcLMWm1, AcLMWm2 and AcLMWm3 from Aegilops cylindrica Host (2n = 4x = 14, CCDD). The coding regions of AmLMWm1, AcLMWm1, AcLMWm2 and AcLMWm3 were 1,092, 1,119, 912 and 936 bp in length, encoding 39,168, 40,297, 31,961 and 33,396 Da LMW-GS, respectively. In order to confirm their authenticity, these LMW-GS genes were successfully expressed in E.coli. The four novel genes belong to LMW-m types and, according to the first and seventh cysteine positions, were further classified as types III, I, IV and V, respectively. Among these novel genes, AmLMWm1 and AcLMWm1 possessed a longer repetitive domain (20 and 22 repeats) than common LMW-GS genes, which was considered to be associated with good dough quality of wheat. Phylogenetic analysis showed C and D genomes of Aegilops involved in this study had LMW-GS loci similar to those of the A, B, and D genomes in common wheat.

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Cloning, expression and characterization of novel avenin-like genes in wheat and related species

Cited by 23 publications

References 24 publications

Abiotic Stress Resistance, a Novel Moonlighting Function of Ribosomal Protein RPL44 in the Halophilic Fungus Aspergillus glaucus

Abiotic Stress Resistance, a Novel Moonlighting Function of Ribosomal Protein RPL44 in the Halophilic Fungus Aspergillus glaucus

Molecular characterization and evolutionary origins of farinin genes in Brachypodium distachyon L.

Cloning and characterization of novel low molecular weight glutenin subunit genes from two Aegilops species with the C and D genomes

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