Molecular and biochemical characterisation of a novel type II peroxiredoxin (XvPrx2) from the resurrection plant Xerophyta viscosa.
Identifieur interne : 000442 ( Main/Exploration ); précédent : 000441; suivant : 000443Molecular and biochemical characterisation of a novel type II peroxiredoxin (XvPrx2) from the resurrection plant Xerophyta viscosa.
Auteurs : Kershini Govender [Afrique du Sud] ; Jennifer A. Thomson [Afrique du Sud] ; Sagadevan Mundree [Australie] ; Abdelaleim Ismail Elsayed [Égypte] ; Mohammed Suhail Rafudeen [Afrique du Sud]Source :
- Functional plant biology : FPB [ 1445-4416 ] ; 2016.
Abstract
A type II peroxiredoxin gene (XvPrx2) was isolated from a Xerophyta viscosa (Baker) cDNA cold-stress library. The polypeptide displayed significant similarity to other plant type II peroxiredoxins, with the conserved amino acid motif (PGAFTPTCS) proposed to constitute the active site of the enzyme. Northern blot analyses showed that XvPrx2 gene was stress-inducible in response to abiotic stresses while gel analyses revealed that XvPrx2 homologues exist within the X. viscosa proteome. Using a yellow fluorescent reporter protein, the XvPrx2 protein localised to the cytosol. A mutated protein (XvV7) was generated by converting the valine at position 76 to a cysteine and an in vitro DNA protection assay showed that, in the presence of either XvPrx2 or XvV7, DNA protection occurred. In addition, an in vivo assay showed that increased protection was conferred to Escherichia coli cells overexpressing either XvPrx2 or XvV7. The XvPrx2 activity was maximal with DTT as electron donor and H2O2 as substrate. Using E. coli thioredoxin, a 2-15-fold lower enzyme activity was observed. The XvPrx2 activity with glutathione was significantly lower and glutaredoxin had no measurable effect on this reaction. The XvV7 protein displayed significantly lower activity compared with XvPrx2 for all substrates assessed.
DOI: 10.1071/FP15291
PubMed: 32480495
Affiliations:
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The polypeptide displayed significant similarity to other plant type II peroxiredoxins, with the conserved amino acid motif (PGAFTPTCS) proposed to constitute the active site of the enzyme. Northern blot analyses showed that XvPrx2 gene was stress-inducible in response to abiotic stresses while gel analyses revealed that XvPrx2 homologues exist within the X. viscosa proteome. Using a yellow fluorescent reporter protein, the XvPrx2 protein localised to the cytosol. A mutated protein (XvV7) was generated by converting the valine at position 76 to a cysteine and an in vitro DNA protection assay showed that, in the presence of either XvPrx2 or XvV7, DNA protection occurred. In addition, an in vivo assay showed that increased protection was conferred to Escherichia coli cells overexpressing either XvPrx2 or XvV7. The XvPrx2 activity was maximal with DTT as electron donor and H2O2 as substrate. Using E. coli thioredoxin, a 2-15-fold lower enzyme activity was observed. The XvPrx2 activity with glutathione was significantly lower and glutaredoxin had no measurable effect on this reaction. The XvV7 protein displayed significantly lower activity compared with XvPrx2 for all substrates assessed.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32480495</PMID><DateRevised><Year>2020</Year><Month>06</Month><Day>02</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1445-4416</ISSN><JournalIssue CitedMedium="Internet"><Volume>43</Volume><Issue>7</Issue><PubDate><Year>2016</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Functional plant biology : FPB</Title><ISOAbbreviation>Funct Plant Biol</ISOAbbreviation></Journal><ArticleTitle>Molecular and biochemical characterisation of a novel type II peroxiredoxin (XvPrx2) from the resurrection plant Xerophyta viscosa.</ArticleTitle><Pagination><MedlinePgn>669-683</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1071/FP15291</ELocationID><Abstract><AbstractText>A type II peroxiredoxin gene (XvPrx2) was isolated from a Xerophyta viscosa (Baker) cDNA cold-stress library. The polypeptide displayed significant similarity to other plant type II peroxiredoxins, with the conserved amino acid motif (PGAFTPTCS) proposed to constitute the active site of the enzyme. Northern blot analyses showed that XvPrx2 gene was stress-inducible in response to abiotic stresses while gel analyses revealed that XvPrx2 homologues exist within the X. viscosa proteome. Using a yellow fluorescent reporter protein, the XvPrx2 protein localised to the cytosol. A mutated protein (XvV7) was generated by converting the valine at position 76 to a cysteine and an in vitro DNA protection assay showed that, in the presence of either XvPrx2 or XvV7, DNA protection occurred. In addition, an in vivo assay showed that increased protection was conferred to Escherichia coli cells overexpressing either XvPrx2 or XvV7. The XvPrx2 activity was maximal with DTT as electron donor and H2O2 as substrate. Using E. coli thioredoxin, a 2-15-fold lower enzyme activity was observed. The XvPrx2 activity with glutathione was significantly lower and glutaredoxin had no measurable effect on this reaction. The XvV7 protein displayed significantly lower activity compared with XvPrx2 for all substrates assessed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Govender</LastName><ForeName>Kershini</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, University of Cape Town, Private Bag, Rondebosch, 7701, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thomson</LastName><ForeName>Jennifer A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, University of Cape Town, Private Bag, Rondebosch, 7701, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mundree</LastName><ForeName>Sagadevan</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centre for Tropical Crops and Biocommodities, Queensland University of Technology, PO Box 2434, Brisbane, Qld 4001, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>ElSayed</LastName><ForeName>Abdelaleim Ismail</ForeName><Initials>AI</Initials><AffiliationInfo><Affiliation>Biochemistry Department, Faculty of Agriculture, Zagazig University, 44519 Zagazig, Egypt.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rafudeen</LastName><ForeName>Mohammed Suhail</ForeName><Initials>MS</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, University of Cape Town, Private Bag, Rondebosch, 7701, South Africa.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Australia</Country><MedlineTA>Funct Plant Biol</MedlineTA><NlmUniqueID>101154361</NlmUniqueID><ISSNLinking>1445-4416</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>09</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>11</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>6</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32480495</ArticleId><ArticleId IdType="pii">FP15291</ArticleId><ArticleId IdType="doi">10.1071/FP15291</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Afrique du Sud</li><li>Australie</li><li>Égypte</li></country></list><tree><country name="Afrique du Sud"><noRegion><name sortKey="Govender, Kershini" sort="Govender, Kershini" uniqKey="Govender K" first="Kershini" last="Govender">Kershini Govender</name></noRegion><name sortKey="Rafudeen, Mohammed Suhail" sort="Rafudeen, Mohammed Suhail" uniqKey="Rafudeen M" first="Mohammed Suhail" last="Rafudeen">Mohammed Suhail Rafudeen</name><name sortKey="Thomson, Jennifer A" sort="Thomson, Jennifer A" uniqKey="Thomson J" first="Jennifer A" last="Thomson">Jennifer A. Thomson</name></country><country name="Australie"><noRegion><name sortKey="Mundree, Sagadevan" sort="Mundree, Sagadevan" uniqKey="Mundree S" first="Sagadevan" last="Mundree">Sagadevan Mundree</name></noRegion></country><country name="Égypte"><noRegion><name sortKey="Elsayed, Abdelaleim Ismail" sort="Elsayed, Abdelaleim Ismail" uniqKey="Elsayed A" first="Abdelaleim Ismail" last="Elsayed">Abdelaleim Ismail Elsayed</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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