Cloning, characterization, and bacterial over-expression of an osmotin-like protein gene from Solanum nigrum L. with antifungal activity against three necrotrophic fungi.
Identifieur interne : 000148 ( Main/Corpus ); précédent : 000147; suivant : 000149Cloning, characterization, and bacterial over-expression of an osmotin-like protein gene from Solanum nigrum L. with antifungal activity against three necrotrophic fungi.
Auteurs : Supriyo Chowdhury ; Arpita Basu ; Surekha KunduSource :
- Molecular biotechnology [ 1559-0305 ] ; 2015.
English descriptors
- KwdEn :
- Antifungal Agents (chemistry), Antifungal Agents (metabolism), Antifungal Agents (pharmacology), Cell Membrane (metabolism), Cloning, Molecular (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Fungi (cytology), Fungi (drug effects), Fungi (metabolism), Hydrogen-Ion Concentration (MeSH), Microbial Sensitivity Tests (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Plant Proteins (pharmacology), Protein Stability (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Recombinant Proteins (pharmacology), Solanum nigrum (genetics).
- MESH :
- chemical , chemistry : Antifungal Agents, Plant Proteins, Recombinant Proteins.
- chemical , genetics : Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Antifungal Agents, Plant Proteins, Recombinant Proteins.
- chemical , pharmacology : Antifungal Agents, Plant Proteins, Recombinant Proteins.
- cytology : Fungi.
- drug effects : Fungi.
- genetics : Escherichia coli, Solanum nigrum.
- metabolism : Cell Membrane, Escherichia coli, Fungi.
- Cloning, Molecular, Hydrogen-Ion Concentration, Microbial Sensitivity Tests, Protein Stability.
Abstract
A new osmotin-like protein gene from Solanum nigrum L. var indica (SindOLP) was cloned and overexpressed in Escherichia coli. The full-length intron-less gene is 744 bp, encoding a mature protein of 247 amino acids with a molecular mass of 26 kDa. The protein has an N-terminal cleavable signal sequence of 21 amino acids. There is the Thaumatin family signature pattern, with one each of amidation, N-myristoylation, casein kinase II phosphorylation, tyrosine kinase phosphorylation, and protein kinase C phosphorylation sites. Hydropathy plot showed that it has six transmembrane helices. It has antifungal activity and can permeabilize fungal hyphae and spores. SindOLP is most active at pH 8, 25 °C and its antifungal activity is retained after 75 °C for 30 min. SindOLP inhibits fungal spore germination. The protein however lacks glucanase activity. The potential for SindOLP in developing fungus-resistant, transgenic crops is discussed.
DOI: 10.1007/s12033-014-9831-4
PubMed: 25572937
Links to Exploration step
pubmed:25572937Le document en format XML
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The full-length intron-less gene is 744 bp, encoding a mature protein of 247 amino acids with a molecular mass of 26 kDa. The protein has an N-terminal cleavable signal sequence of 21 amino acids. There is the Thaumatin family signature pattern, with one each of amidation, N-myristoylation, casein kinase II phosphorylation, tyrosine kinase phosphorylation, and protein kinase C phosphorylation sites. Hydropathy plot showed that it has six transmembrane helices. It has antifungal activity and can permeabilize fungal hyphae and spores. SindOLP is most active at pH 8, 25 °C and its antifungal activity is retained after 75 °C for 30 min. SindOLP inhibits fungal spore germination. The protein however lacks glucanase activity. The potential for SindOLP in developing fungus-resistant, transgenic crops is discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25572937</PMID><DateCompleted><Year>2015</Year><Month>12</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1559-0305</ISSN><JournalIssue CitedMedium="Internet"><Volume>57</Volume><Issue>4</Issue><PubDate><Year>2015</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Molecular biotechnology</Title><ISOAbbreviation>Mol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Cloning, characterization, and bacterial over-expression of an osmotin-like protein gene from Solanum nigrum L. with antifungal activity against three necrotrophic fungi.</ArticleTitle><Pagination><MedlinePgn>371-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12033-014-9831-4</ELocationID><Abstract><AbstractText>A new osmotin-like protein gene from Solanum nigrum L. var indica (SindOLP) was cloned and overexpressed in Escherichia coli. The full-length intron-less gene is 744 bp, encoding a mature protein of 247 amino acids with a molecular mass of 26 kDa. The protein has an N-terminal cleavable signal sequence of 21 amino acids. There is the Thaumatin family signature pattern, with one each of amidation, N-myristoylation, casein kinase II phosphorylation, tyrosine kinase phosphorylation, and protein kinase C phosphorylation sites. Hydropathy plot showed that it has six transmembrane helices. It has antifungal activity and can permeabilize fungal hyphae and spores. SindOLP is most active at pH 8, 25 °C and its antifungal activity is retained after 75 °C for 30 min. SindOLP inhibits fungal spore germination. The protein however lacks glucanase activity. 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