Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins

Tanchak, Michael A.; Schernthaner, Johann P.; Giband, Marc; Altosaar, Illimar

doi:10.1016/s0168-9452(98)00105-8

Cited by 36 publications

(18 citation statements)

References 17 publications

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“…The conservation of Puroindoline-a DNA sequences is particularly high between wheat, rye and oat, ranging from 99.3 to 100%. In oat, two groups of puroindoline-like proteins were reported, which are: avenoindolines (Gautier et al 2000) and tryptophanins (Tanchak et al 1998). Avenoindolines were found to be more closely related to puroindolines than tryptophanins.…”

Section: Avenoindoline-a Avenoindoline-bmentioning

confidence: 99%

“…This group of proteins is encoded by a multi-gene family. Cross-hybridizing RNAs of puroindolines are also present in developing wheat rye and barley seeds, but not in rice seeds (Tanchak et al 1998). Similar to rice, puroindoline-like genes are absent in maize and sorghum, which do not have a soft endosperm, with the exception for the specific mutants opaque-2 and zeins in maize.…”

Section: Avenoindoline-a Avenoindoline-bmentioning

confidence: 99%

“…The tryptophanrich domain is highly hydrophobic and has an affinity for binding lipids (Wilde et al 1993;Dubreil et al 1997). Isoforms of puroindolines a and b are present in the starch endosperm of the Triticeae and Aveneae tribes (Morris 2002) and are synthesized specifically in the endosperm during the kernel development of wheat (Gautier et al 1994;Dubreil et al 1998a), oat (Tanchak et al 1998), and barley (Darlington et al 2000). The interaction of puroindolines with starch granules and with biological membranes is responsible for their specific properties, such as endosperm softening and antimicrobial activity (Blochet et al 1993;Krishnamurthy et al 2001a;Morris 2002).…”

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The determinants of grain texture in cereals

2009

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Kernel hardness is an important agronomic trait that influences end-product properties. In wheat cultivars, this trait is determined by the Puroindoline a (Pina) and Puroindoline b (Pinb) genes, located in the Hardness locus (Ha) on chromosome 5DS of the D genome. Wild type alleles code puroindoline a (PINA) and puroindoline b (PINB) proteins, which form a 15-kDa friabilin present on the surface of water-washed starch granules. Both the proteins are accumulated in the starch endosperm cells and aleurone of the mature kernels. Puroindoline-like genes coding puroindoline-like proteins in the starch endosperm occur in some of the genomes of Triticeae and Aveneae cereals. Orthologs are present in barley, rye and oats. However, some genomes of these diploid and polyploid cereals, like that of Triticum turgidum var. durum (AABB) lack the puroindoline genes, having a very hard kernel texture. The two wild type alleles in opposition (dominant loci) control the soft phenotype. Mutation either in Pina or Pinb or in both leads to a medium-hard or hard kernel texture. The most frequent types of Pin mutations are point mutations within the coding sequence resulting in the substitution of a single amino acid or a null allele. The latter is the result of a frame shift determined by base deletion or insertion or a one-point mutation to the stop codon. The lipid-binding properties of the puroindolines affect not only the dough quality but also the plants' resistance to pathogens. Genetic modification of cereals with Puroindoline genes and/or their promoters enable more detailed functional analyses and the production of plants with the desired characteristics.

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Section: Avenoindoline-a Avenoindoline-bmentioning

confidence: 99%

Section: Avenoindoline-a Avenoindoline-bmentioning

confidence: 99%

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confidence: 99%

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The determinants of grain texture in cereals

2009

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“…In addition, the wheat puroindoline genes have been found to affect the endosperm texture of transformed rice when expressed as transgenes (Krishnamurthy and Giroux 2001). Puroindoline-like sequences were found in other members of the Triticeae tribe (Gautier et al 2000, Simone andLafiandra 2005) and oats (Tanchak et al 1998). However, there are few studies on either the expression or allelic variation of puroindoline orthologs in species other than wheat.…”

Section: Discussionmentioning

confidence: 99%

Hordoindolines are Predominantly Expressed in the Aleurone Layer in Late Kernel Development in Barley

et al. 2006

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In order to isolate grain-specific genes during kernel development, two differential screening methods-suppression subtractive hybridization (SSH) and differential hybridization (DH)-were applied. Two cDNAs encoding hordoindolines known to be related to grain hardness were isolated and designated as Hordeum vulgare indoline a and b (HvIDa and HvIDb). The cDNAs encoding HvIDa and HvIDb contained a 450 bp and a 444 bp open reading frame (ORF) that encoded the putative hordoindoline-a and -b precursors consisting of 150 and 148 amino acids, respectively. The deduced amino acid sequences of both HvIDa and HvIDb contained one tryptophan-rich domain and ten highly conserved cysteine residues. The expression of the HvIDa gene was high at 5 DAF, reached a peak at 8 DAF and decreased slightly until 20 DAF, while the expression of HvIDb began to be detectable at 8 DAF when it was higher than that of other developmental stages and decreased slightly until 20 DAF. The HvIDa and HvIDb genes were predominantly detected in the aleurone cell layers in the late part of kernel development, e.g. at 20 DAF. These findings may provide clues to the molecular mechanisms of kernel development and contribute to the determination of the grain texture in barley.

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“…These tryptophan residues are critical for the binding of GSP and puroindolines to lipids, which is the reason they affect grain texture. Isolation and molecular characterization of oat complementary DNA clones encoding proteins structurally related to wheat GSP have been evaluated (Tanchak et al, 1998) and have shown that tryptophanins (the name used for GSP and puroindolines in the study) were present in oat, wheat, barley, and rye but not in developing rice seed. Because these variations occur in the first part of the sequence under study, they can be created by error in the sequencing system.…”

Section: Wheat Gspmentioning

confidence: 99%

Identification and sequence analysis of grain softness protein in selected wheat, rye and triticale

Kharrazi¹,

Bobojonov²

2012

Genet. Mol. Res.

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ABSTRACT. Grain softness protein (GSP) is an important protein for overcoming milling and grain defenses in the innate immunity systems of cereals. The objective of this study was to evaluate and understand GSP sequences in selected wheat, rye and triticale. Using sequences for this gene from a sequence database, we performed clustering analysis to compare the sequences obtained from 3 germplasms with other studied sequences for GSP. The maximum difference between the Hirmand GSP genotype in wheat and the database sequences was 23% in EF109396 and EF109399. Most amino acid variation between the GSP sequences involved the same amino acids. The Nikita rye GSP gene showed 64% identity with DQ269918 and AY667063. The isoelectric point in the GSP of wheat and Lasko triticale was significantly higher than that of rye GSP. In addition, parameters such as optical density, grand average of hydrophobicity, percentage of hydrophobicity and hydrophilic amino acids, and number of alpha helices and beta sheets in GSP were similar in wheat and triticale but not in wheat and rye.

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Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins

Cited by 36 publications

References 17 publications

The determinants of grain texture in cereals

The determinants of grain texture in cereals

Hordoindolines are Predominantly Expressed in the Aleurone Layer in Late Kernel Development in Barley

Identification and sequence analysis of grain softness protein in selected wheat, rye and triticale

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