Gene expression and characterization of isoprene synthase from Populus alba.
Identifieur interne : 004075 ( Main/Corpus ); précédent : 004074; suivant : 004076Gene expression and characterization of isoprene synthase from Populus alba.
Auteurs : Kanako Sasaki ; Kazuaki Ohara ; Kazufumi YazakiSource :
- FEBS letters [ 0014-5793 ] ; 2005.
English descriptors
- KwdEn :
- Alkyl and Aryl Transferases (genetics), Alkyl and Aryl Transferases (metabolism), Cloning, Molecular (MeSH), DNA, Complementary (genetics), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Hydrogen-Ion Concentration (MeSH), Populus (enzymology), Populus (genetics), Protein Transport (MeSH), RNA, Messenger (genetics), RNA, Messenger (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Analysis, DNA (MeSH), Temperature (MeSH).
- MESH :
- chemical , genetics : Alkyl and Aryl Transferases, DNA, Complementary, RNA, Messenger, Recombinant Proteins.
- chemical , metabolism : Alkyl and Aryl Transferases, RNA, Messenger, Recombinant Proteins.
- enzymology : Populus.
- genetics : Populus.
- Cloning, Molecular, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Hydrogen-Ion Concentration, Protein Transport, Sequence Analysis, DNA, Temperature.
Abstract
Isoprene synthase cDNA from Populus alba (PaIspS) was isolated by RT-PCR. This PaIspS mRNA, which was predominantly observed in the leaves, was strongly induced by heat stress and continuous light irradiation, and was substantially decreased in the dark, suggesting that isoprene emission was regulated at the transcriptional level. The subcellular localization of PaIspS protein with green fluorescent protein fusion was shown to be in plastids. PaIspS expressed in Escherichia coli was characterized enzymatically: it had an optimum pH of approximately 8.0, and an optimum temperature 40 degrees C. Its preference for divalent cations for its activity was also studied.
DOI: 10.1016/j.febslet.2005.03.066
PubMed: 15848197
Links to Exploration step
pubmed:15848197Le document en format XML
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This PaIspS mRNA, which was predominantly observed in the leaves, was strongly induced by heat stress and continuous light irradiation, and was substantially decreased in the dark, suggesting that isoprene emission was regulated at the transcriptional level. The subcellular localization of PaIspS protein with green fluorescent protein fusion was shown to be in plastids. PaIspS expressed in Escherichia coli was characterized enzymatically: it had an optimum pH of approximately 8.0, and an optimum temperature 40 degrees C. Its preference for divalent cations for its activity was also studied.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15848197</PMID><DateCompleted><Year>2005</Year><Month>05</Month><Day>31</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>579</Volume><Issue>11</Issue><PubDate><Year>2005</Year><Month>Apr</Month><Day>25</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Gene expression and characterization of isoprene synthase from Populus alba.</ArticleTitle><Pagination><MedlinePgn>2514-8</MedlinePgn></Pagination><Abstract><AbstractText>Isoprene synthase cDNA from Populus alba (PaIspS) was isolated by RT-PCR. This PaIspS mRNA, which was predominantly observed in the leaves, was strongly induced by heat stress and continuous light irradiation, and was substantially decreased in the dark, suggesting that isoprene emission was regulated at the transcriptional level. The subcellular localization of PaIspS protein with green fluorescent protein fusion was shown to be in plastids. PaIspS expressed in Escherichia coli was characterized enzymatically: it had an optimum pH of approximately 8.0, and an optimum temperature 40 degrees C. 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