A dehydration-inducible gene in the truffle Tuber borchii identifies a novel group of dehydrins.
Identifieur interne : 003333 ( Main/Corpus ); précédent : 003332; suivant : 003334A dehydration-inducible gene in the truffle Tuber borchii identifies a novel group of dehydrins.
Auteurs : Simona Abba' ; Stefano Ghignone ; Paola BonfanteSource :
- BMC genomics [ 1471-2164 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Bayes Theorem (MeSH), Cold Temperature (MeSH), Computational Biology (MeSH), Conserved Sequence (MeSH), Dehydration (genetics), Expressed Sequence Tags (MeSH), Genes, Fungal (MeSH), Hordeum (genetics), Molecular Sequence Data (MeSH), Mycorrhizae (genetics), Osmotic Pressure (MeSH), Phylogeny (MeSH), Plant Proteins (classification), Plant Proteins (genetics), Plant Proteins (isolation & purification), Sequence Analysis (MeSH), Sequence Homology, Amino Acid (MeSH), Tissue Distribution (MeSH).
- MESH :
- chemical , classification : Plant Proteins.
- genetics : Dehydration, Hordeum, Mycorrhizae, Plant Proteins.
- chemical , isolation & purification : Plant Proteins.
- Amino Acid Sequence, Base Sequence, Bayes Theorem, Cold Temperature, Computational Biology, Conserved Sequence, Expressed Sequence Tags, Genes, Fungal, Molecular Sequence Data, Osmotic Pressure, Phylogeny, Sequence Analysis, Sequence Homology, Amino Acid, Tissue Distribution.
Abstract
BACKGROUND
The expressed sequence tag M6G10 was originally isolated from a screening for differentially expressed transcripts during the reproductive stage of the white truffle Tuber borchii. mRNA levels for M6G10 increased dramatically during fruiting body maturation compared to the vegetative mycelial stage.
RESULTS
Bioinformatics tools, phylogenetic analysis and expression studies were used to support the hypothesis that this sequence, named TbDHN1, is the first dehydrin (DHN)-like coding gene isolated in fungi. Homologs of this gene, all defined as "coding for hypothetical proteins" in public databases, were exclusively found in ascomycetous fungi and in plants. Although complete (or almost complete) fungal genomes and EST collections of some Basidiomycota and Glomeromycota are already available, DHN-like proteins appear to be represented only in Ascomycota. A new and previously uncharacterized conserved signature pattern was identified and proposed to Uniprot database as the main distinguishing feature of this new group of DHNs. Expression studies provide experimental evidence of a transcript induction of TbDHN1 during cellular dehydration.
CONCLUSION
Expression pattern and sequence similarities to known plant DHNs indicate that TbDHN1 is the first characterized DHN-like protein in fungi. The high similarity of TbDHN1 with homolog coding sequences implies the existence of a novel fungal/plant group of LEA Class II proteins characterized by a previously undescribed signature pattern.
DOI: 10.1186/1471-2164-7-39
PubMed: 16512918
PubMed Central: PMC1550403
Links to Exploration step
pubmed:16512918Le document en format XML
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<affiliation><nlm:affiliation>Dipartimento di Biologia Vegetale dell'Università degli Studi di Torino and IPP-CNR-Sezione di Torino, Viale Mattioli 25, 10125 Torino, Italy. simona.abba@unito.it</nlm:affiliation>
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<affiliation><nlm:affiliation>Dipartimento di Biologia Vegetale dell'Università degli Studi di Torino and IPP-CNR-Sezione di Torino, Viale Mattioli 25, 10125 Torino, Italy. simona.abba@unito.it</nlm:affiliation>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Bayes Theorem (MeSH)</term>
<term>Cold Temperature (MeSH)</term>
<term>Computational Biology (MeSH)</term>
<term>Conserved Sequence (MeSH)</term>
<term>Dehydration (genetics)</term>
<term>Expressed Sequence Tags (MeSH)</term>
<term>Genes, Fungal (MeSH)</term>
<term>Hordeum (genetics)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mycorrhizae (genetics)</term>
<term>Osmotic Pressure (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Plant Proteins (classification)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (isolation & purification)</term>
<term>Sequence Analysis (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Tissue Distribution (MeSH)</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Dehydration</term>
<term>Hordeum</term>
<term>Mycorrhizae</term>
<term>Plant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Plant Proteins</term>
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<term>Bayes Theorem</term>
<term>Cold Temperature</term>
<term>Computational Biology</term>
<term>Conserved Sequence</term>
<term>Expressed Sequence Tags</term>
<term>Genes, Fungal</term>
<term>Molecular Sequence Data</term>
<term>Osmotic Pressure</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>The expressed sequence tag M6G10 was originally isolated from a screening for differentially expressed transcripts during the reproductive stage of the white truffle Tuber borchii. mRNA levels for M6G10 increased dramatically during fruiting body maturation compared to the vegetative mycelial stage.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>Bioinformatics tools, phylogenetic analysis and expression studies were used to support the hypothesis that this sequence, named TbDHN1, is the first dehydrin (DHN)-like coding gene isolated in fungi. Homologs of this gene, all defined as "coding for hypothetical proteins" in public databases, were exclusively found in ascomycetous fungi and in plants. Although complete (or almost complete) fungal genomes and EST collections of some Basidiomycota and Glomeromycota are already available, DHN-like proteins appear to be represented only in Ascomycota. A new and previously uncharacterized conserved signature pattern was identified and proposed to Uniprot database as the main distinguishing feature of this new group of DHNs. Expression studies provide experimental evidence of a transcript induction of TbDHN1 during cellular dehydration.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSION</b>
</p>
<p>Expression pattern and sequence similarities to known plant DHNs indicate that TbDHN1 is the first characterized DHN-like protein in fungi. The high similarity of TbDHN1 with homolog coding sequences implies the existence of a novel fungal/plant group of LEA Class II proteins characterized by a previously undescribed signature pattern.</p>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">The expressed sequence tag M6G10 was originally isolated from a screening for differentially expressed transcripts during the reproductive stage of the white truffle Tuber borchii. mRNA levels for M6G10 increased dramatically during fruiting body maturation compared to the vegetative mycelial stage.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">Bioinformatics tools, phylogenetic analysis and expression studies were used to support the hypothesis that this sequence, named TbDHN1, is the first dehydrin (DHN)-like coding gene isolated in fungi. Homologs of this gene, all defined as "coding for hypothetical proteins" in public databases, were exclusively found in ascomycetous fungi and in plants. Although complete (or almost complete) fungal genomes and EST collections of some Basidiomycota and Glomeromycota are already available, DHN-like proteins appear to be represented only in Ascomycota. A new and previously uncharacterized conserved signature pattern was identified and proposed to Uniprot database as the main distinguishing feature of this new group of DHNs. Expression studies provide experimental evidence of a transcript induction of TbDHN1 during cellular dehydration.</AbstractText>
<AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">Expression pattern and sequence similarities to known plant DHNs indicate that TbDHN1 is the first characterized DHN-like protein in fungi. The high similarity of TbDHN1 with homolog coding sequences implies the existence of a novel fungal/plant group of LEA Class II proteins characterized by a previously undescribed signature pattern.</AbstractText>
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