Arsenic metalation of seaweed Fucus vesiculosus metallothionein: the importance of the interdomain linker in metallothionein.
Identifieur interne : 000262 ( Main/Exploration ); précédent : 000261; suivant : 000263Arsenic metalation of seaweed Fucus vesiculosus metallothionein: the importance of the interdomain linker in metallothionein.
Auteurs : Thanh T. Ngu [Canada] ; Janice A. Lee ; Moira K. Rushton ; Martin J. StillmanSource :
- Biochemistry [ 1520-4995 ] ; 2009.
Descripteurs français
- KwdFr :
- Arsenic (composition chimique), Arsenic (métabolisme), Arsenic (toxicité), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Fucus (composition chimique), Fucus (effets des médicaments et des substances chimiques), Fucus (métabolisme), Liaison aux protéines (MeSH), Métallothionéine (composition chimique), Métallothionéine (métabolisme), Protéines d'algue (composition chimique), Protéines d'algue (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Spectrométrie de masse ESI (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Arsenic, Fucus, Métallothionéine, Protéines d'algue, Protéines recombinantes.
- effets des médicaments et des substances chimiques : Fucus.
- métabolisme : Arsenic, Fucus, Métallothionéine, Protéines d'algue, Protéines recombinantes.
- toxicité : Arsenic.
- Cinétique, Données de séquences moléculaires, Liaison aux protéines, Spectrométrie de masse ESI, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Algal Proteins (metabolism), Amino Acid Sequence (MeSH), Arsenic (chemistry), Arsenic (metabolism), Arsenic (toxicity), Fucus (chemistry), Fucus (drug effects), Fucus (metabolism), Kinetics (MeSH), Metallothionein (chemistry), Metallothionein (metabolism), Molecular Sequence Data (MeSH), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Spectrometry, Mass, Electrospray Ionization (MeSH).
- MESH :
- chemical , chemistry : Algal Proteins, Arsenic, Metallothionein, Recombinant Proteins.
- chemical , metabolism : Algal Proteins, Arsenic, Metallothionein, Recombinant Proteins.
- chemical , toxicity : Arsenic.
- chemistry : Fucus.
- drug effects : Fucus.
- metabolism : Fucus.
- Amino Acid Sequence, Kinetics, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Spectrometry, Mass, Electrospray Ionization.
Abstract
The presence of metallothionein in seaweed Fucus vesiculosus has been suggested as the protecting agent against toxic metals in the contaminated waters it can grow in. We report the first kinetic pathway data for A3+ binding to an algal metallothionein, F. vesiculosus metallothionein (rfMT). The time and temperature dependence of the relative concentrations of apo-rfMT and the five As-containing species have been determined following mixing of As3+ and apo-rfMT using electrospray ionization mass spectrometry (ESI MS). Kinetic analysis of the detailed time-resolved mass spectral data for As3+ metalation allows the simulation of the metalation reactions showing the consumption of apo-rfMT, the formation and consumption of As1- to As4-rfMT, and subsequent, final formation of As5-rfMT. The kinetic model proposed here provides a stepwise analysis of the metalation reaction showing time-resolved occupancy of the Cys7 and the Cys9 domain. The rate constants (M(-1) s(-1)) calculated from the fits for the 7-cysteine gamma domain are k1gamma, 19.8, and k2gamma, 1.4, and for the 9-cysteine beta domain are k1beta, 16.3, k2beta, 9.1, and k3beta, 2.2. The activation energies and Arrhenius factors for each of the reaction steps are also reported. rfMT has a long 14 residue linker, which as we show from analysis of the ESI MS data, allows each of its two domains to bind As3+ independently of each other. The analysis provides for the first time an explanation of the differing metal-binding properties of two-domain MTs with linkers of varying lengths, suggesting further comparison between plant (with long linkers) and mammalian (with short linkers) metallothioneins will shed light on the role of the interdomain linker.
DOI: 10.1021/bi9007462
PubMed: 19655782
Affiliations:
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We report the first kinetic pathway data for A3+ binding to an algal metallothionein, F. vesiculosus metallothionein (rfMT). The time and temperature dependence of the relative concentrations of apo-rfMT and the five As-containing species have been determined following mixing of As3+ and apo-rfMT using electrospray ionization mass spectrometry (ESI MS). Kinetic analysis of the detailed time-resolved mass spectral data for As3+ metalation allows the simulation of the metalation reactions showing the consumption of apo-rfMT, the formation and consumption of As1- to As4-rfMT, and subsequent, final formation of As5-rfMT. The kinetic model proposed here provides a stepwise analysis of the metalation reaction showing time-resolved occupancy of the Cys7 and the Cys9 domain. The rate constants (M(-1) s(-1)) calculated from the fits for the 7-cysteine gamma domain are k1gamma, 19.8, and k2gamma, 1.4, and for the 9-cysteine beta domain are k1beta, 16.3, k2beta, 9.1, and k3beta, 2.2. The activation energies and Arrhenius factors for each of the reaction steps are also reported. rfMT has a long 14 residue linker, which as we show from analysis of the ESI MS data, allows each of its two domains to bind As3+ independently of each other. The analysis provides for the first time an explanation of the differing metal-binding properties of two-domain MTs with linkers of varying lengths, suggesting further comparison between plant (with long linkers) and mammalian (with short linkers) metallothioneins will shed light on the role of the interdomain linker.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19655782</PMID><DateCompleted><Year>2009</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>48</Volume><Issue>37</Issue><PubDate><Year>2009</Year><Month>Sep</Month><Day>22</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Arsenic metalation of seaweed Fucus vesiculosus metallothionein: the importance of the interdomain linker in metallothionein.</ArticleTitle><Pagination><MedlinePgn>8806-16</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/bi9007462</ELocationID><Abstract><AbstractText>The presence of metallothionein in seaweed Fucus vesiculosus has been suggested as the protecting agent against toxic metals in the contaminated waters it can grow in. We report the first kinetic pathway data for A3+ binding to an algal metallothionein, F. vesiculosus metallothionein (rfMT). The time and temperature dependence of the relative concentrations of apo-rfMT and the five As-containing species have been determined following mixing of As3+ and apo-rfMT using electrospray ionization mass spectrometry (ESI MS). Kinetic analysis of the detailed time-resolved mass spectral data for As3+ metalation allows the simulation of the metalation reactions showing the consumption of apo-rfMT, the formation and consumption of As1- to As4-rfMT, and subsequent, final formation of As5-rfMT. The kinetic model proposed here provides a stepwise analysis of the metalation reaction showing time-resolved occupancy of the Cys7 and the Cys9 domain. The rate constants (M(-1) s(-1)) calculated from the fits for the 7-cysteine gamma domain are k1gamma, 19.8, and k2gamma, 1.4, and for the 9-cysteine beta domain are k1beta, 16.3, k2beta, 9.1, and k3beta, 2.2. The activation energies and Arrhenius factors for each of the reaction steps are also reported. rfMT has a long 14 residue linker, which as we show from analysis of the ESI MS data, allows each of its two domains to bind As3+ independently of each other. The analysis provides for the first time an explanation of the differing metal-binding properties of two-domain MTs with linkers of varying lengths, suggesting further comparison between plant (with long linkers) and mammalian (with short linkers) metallothioneins will shed light on the role of the interdomain linker.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ngu</LastName><ForeName>Thanh T</ForeName><Initials>TT</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Western Ontario, London, Ontario, Canada N6A 5B7.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Janice A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Rushton</LastName><ForeName>Moira K</ForeName><Initials>MK</Initials></Author><Author ValidYN="Y"><LastName>Stillman</LastName><ForeName>Martin J</ForeName><Initials>MJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9038-94-2</RegistryNumber><NameOfSubstance UI="D008668">Metallothionein</NameOfSubstance></Chemical><Chemical><RegistryNumber>N712M78A8G</RegistryNumber><NameOfSubstance UI="D001151">Arsenic</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001151" MajorTopicYN="N">Arsenic</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044645" MajorTopicYN="N">Fucus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008668" MajorTopicYN="N">Metallothionein</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>8</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>8</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>10</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19655782</ArticleId><ArticleId IdType="doi">10.1021/bi9007462</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Lee, Janice A" sort="Lee, Janice A" uniqKey="Lee J" first="Janice A" last="Lee">Janice A. Lee</name><name sortKey="Rushton, Moira K" sort="Rushton, Moira K" uniqKey="Rushton M" first="Moira K" last="Rushton">Moira K. Rushton</name><name sortKey="Stillman, Martin J" sort="Stillman, Martin J" uniqKey="Stillman M" first="Martin J" last="Stillman">Martin J. Stillman</name></noCountry><country name="Canada"><noRegion><name sortKey="Ngu, Thanh T" sort="Ngu, Thanh T" uniqKey="Ngu T" first="Thanh T" last="Ngu">Thanh T. Ngu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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