Variability within a pea core collection of LEAM and HSP22, two mitochondrial seed proteins involved in stress tolerance.
Identifieur interne : 002B81 ( PubMed/Corpus ); précédent : 002B80; suivant : 002B82Variability within a pea core collection of LEAM and HSP22, two mitochondrial seed proteins involved in stress tolerance.
Auteurs : Marie-Hélène Avelange-Macherel ; Nicole Payet ; David Lalanne ; Martine Neveu ; Dimitri Tolleter ; Judith Burstin ; David MacherelSource :
- Plant, cell & environment [ 1365-3040 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Sequence, Genotype, Heat-Shock Proteins (genetics), Heat-Shock Proteins (metabolism), Mitochondria (metabolism), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Peas (genetics), Peas (growth & development), Peas (physiology), Plant Proteins (genetics), Plant Proteins (metabolism), Protein Isoforms, Seeds (metabolism), Sequence Alignment, Stress, Physiological, Temperature.
- MESH :
- chemical , genetics : Heat-Shock Proteins, Mitochondrial Proteins, Plant Proteins.
- chemical , metabolism : Heat-Shock Proteins, Mitochondrial Proteins, Plant Proteins.
- genetics : Peas.
- growth & development : Peas.
- metabolism : Mitochondria, Seeds.
- physiology : Peas.
- Amino Acid Sequence, Genotype, Protein Isoforms, Sequence Alignment, Stress, Physiological, Temperature.
Abstract
LEAM, a late embryogenesis abundant protein, and HSP22, a small heat shock protein, were shown to accumulate in the mitochondria during pea (Pisum sativum L.) seed development, where they are expected to contribute to desiccation tolerance. Here, their expression was examined in seeds of 89 pea genotypes by Western blot analysis. All genotypes expressed LEAM and HSP22 in similar amounts. In contrast with HSP22, LEAM displayed different isoforms according to apparent molecular mass. Each of the 89 genotypes harboured a single LEAM isoform. Genomic and RT-PCR analysis revealed four LEAM genes differing by a small variable indel in the coding region. These variations were consistent with the apparent molecular mass of each isoform. Indels, which occurred in repeated domains, did not alter the main properties of LEAM. Structural modelling indicated that the class A α-helix structure, which allows interactions with the mitochondrial inner membrane in the dry state, was preserved in all isoforms, suggesting functionality is maintained. The overall results point out the essential character of LEAM and HSP22 in pea seeds. LEAM variability is discussed in terms of pea breeding history as well as LEA gene evolution mechanisms.
DOI: 10.1111/pce.12480
PubMed: 25367071
Links to Exploration step
pubmed:25367071Le document en format XML
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<term>Mitochondrial Proteins (genetics)</term>
<term>Mitochondrial Proteins (metabolism)</term>
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<term>Peas (physiology)</term>
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<term>Sequence Alignment</term>
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<term>Temperature</term>
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<front><div type="abstract" xml:lang="en">LEAM, a late embryogenesis abundant protein, and HSP22, a small heat shock protein, were shown to accumulate in the mitochondria during pea (Pisum sativum L.) seed development, where they are expected to contribute to desiccation tolerance. Here, their expression was examined in seeds of 89 pea genotypes by Western blot analysis. All genotypes expressed LEAM and HSP22 in similar amounts. In contrast with HSP22, LEAM displayed different isoforms according to apparent molecular mass. Each of the 89 genotypes harboured a single LEAM isoform. Genomic and RT-PCR analysis revealed four LEAM genes differing by a small variable indel in the coding region. These variations were consistent with the apparent molecular mass of each isoform. Indels, which occurred in repeated domains, did not alter the main properties of LEAM. Structural modelling indicated that the class A α-helix structure, which allows interactions with the mitochondrial inner membrane in the dry state, was preserved in all isoforms, suggesting functionality is maintained. The overall results point out the essential character of LEAM and HSP22 in pea seeds. LEAM variability is discussed in terms of pea breeding history as well as LEA gene evolution mechanisms.</div>
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<Abstract><AbstractText>LEAM, a late embryogenesis abundant protein, and HSP22, a small heat shock protein, were shown to accumulate in the mitochondria during pea (Pisum sativum L.) seed development, where they are expected to contribute to desiccation tolerance. Here, their expression was examined in seeds of 89 pea genotypes by Western blot analysis. All genotypes expressed LEAM and HSP22 in similar amounts. In contrast with HSP22, LEAM displayed different isoforms according to apparent molecular mass. Each of the 89 genotypes harboured a single LEAM isoform. Genomic and RT-PCR analysis revealed four LEAM genes differing by a small variable indel in the coding region. These variations were consistent with the apparent molecular mass of each isoform. Indels, which occurred in repeated domains, did not alter the main properties of LEAM. Structural modelling indicated that the class A α-helix structure, which allows interactions with the mitochondrial inner membrane in the dry state, was preserved in all isoforms, suggesting functionality is maintained. The overall results point out the essential character of LEAM and HSP22 in pea seeds. LEAM variability is discussed in terms of pea breeding history as well as LEA gene evolution mechanisms.</AbstractText>
<CopyrightInformation>© 2014 John Wiley & Sons Ltd.</CopyrightInformation>
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