Identification, cloning and characterisation of a novel copper-metallothionein in tetrahymena pigmentosa. Sequencing of cDNA and expression.
Identifieur interne : 000411 ( Main/Corpus ); précédent : 000410; suivant : 000412Identification, cloning and characterisation of a novel copper-metallothionein in tetrahymena pigmentosa. Sequencing of cDNA and expression.
Auteurs : G. Santovito ; P. Irato ; S. Palermo ; F. Boldrin ; R. Sack ; P. Hunziker ; E L PiccinniSource :
- Protist [ 1434-4610 ] ; 2001.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Copper (metabolism), DNA, Complementary (MeSH), DNA, Protozoan (MeSH), Gene Expression (MeSH), Metallothionein (genetics), Metallothionein (isolation & purification), Metallothionein (metabolism), Molecular Sequence Data (MeSH), Peptides (MeSH), RNA, Messenger (MeSH), Sequence Analysis, DNA (MeSH), Sequence Analysis, Protein (MeSH), Sequence Homology, Amino Acid (MeSH), Tetrahymena (genetics).
- MESH :
- chemical , genetics : Metallothionein.
- chemical , isolation & purification : Metallothionein.
- chemical , metabolism : Copper, Metallothionein.
- genetics : Tetrahymena.
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Complementary, DNA, Protozoan, Gene Expression, Molecular Sequence Data, Peptides, RNA, Messenger, Sequence Analysis, DNA, Sequence Analysis, Protein, Sequence Homology, Amino Acid.
Abstract
The protist Tetrahymena pigmentosa accumulates large amounts of metal ions, particularly cadmium and copper. This capability is linked to the induction of metallothioneins (MTs), cysteine-rich metal-binding proteins found in protists, plants and animals. The present study focuses on a novel inducible MT-isoform isolated from Tetrahymena after exposure to a non-toxic dose of copper. The cDNA sequence was determined utilising the partial peptide sequence of purified protein. The Cu-MT cDNA encodes 96 amino acids containing 28 cysteine residues (29%) arranged in motifs characteristic of the metal-binding regions of vertebrate and invertebrate MTs. Both the amino acid and nucleotide sequences differ, not only from other animal MTs, but also from the previously characterised Tetrahymena Cd-MT. Both MTs contain the structural pattern GTXXXCKCXXCKC, which may be proposed as a conservative sequence of Tetrahymena MTs. Cu-dependent regulation of MT expression was also investigated by measuring MT-mRNA and MT levels. MT synthesis occurs very quickly and MT contents increase with Cu accumulation. The induction of Cu-MT mRNA is very rapid, with no observable lag period, and is characterised by transient fluctuation, similar to that described for Cd-MT mRNA. The data reported here indicate that, also in the unicellular organism Tetrahymena, two very different MT isoforms, which perform different biological functions, are expressed according to the inducing metal, Cu or Cd.
DOI: 10.1078/1434-4610-00061
PubMed: 11693660
Links to Exploration step
pubmed:11693660Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Identification, cloning and characterisation of a novel copper-metallothionein in tetrahymena pigmentosa. Sequencing of cDNA and expression.</title><author><name sortKey="Santovito, G" sort="Santovito, G" uniqKey="Santovito G" first="G" last="Santovito">G. Santovito</name><affiliation><nlm:affiliation>Department of Biology, University of Padova, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Irato, P" sort="Irato, P" uniqKey="Irato P" first="P" last="Irato">P. Irato</name></author><author><name sortKey="Palermo, S" sort="Palermo, S" uniqKey="Palermo S" first="S" last="Palermo">S. Palermo</name></author><author><name sortKey="Boldrin, F" sort="Boldrin, F" uniqKey="Boldrin F" first="F" last="Boldrin">F. Boldrin</name></author><author><name sortKey="Sack, R" sort="Sack, R" uniqKey="Sack R" first="R" last="Sack">R. Sack</name></author><author><name sortKey="Hunziker, P" sort="Hunziker, P" uniqKey="Hunziker P" first="P" last="Hunziker">P. Hunziker</name></author><author><name sortKey="Piccinni, E L" sort="Piccinni, E L" uniqKey="Piccinni E" first="E L" last="Piccinni">E L Piccinni</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11693660</idno><idno type="pmid">11693660</idno><idno type="doi">10.1078/1434-4610-00061</idno><idno type="wicri:Area/Main/Corpus">000411</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000411</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification, cloning and characterisation of a novel copper-metallothionein in tetrahymena pigmentosa. Sequencing of cDNA and expression.</title><author><name sortKey="Santovito, G" sort="Santovito, G" uniqKey="Santovito G" first="G" last="Santovito">G. Santovito</name><affiliation><nlm:affiliation>Department of Biology, University of Padova, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Irato, P" sort="Irato, P" uniqKey="Irato P" first="P" last="Irato">P. Irato</name></author><author><name sortKey="Palermo, S" sort="Palermo, S" uniqKey="Palermo S" first="S" last="Palermo">S. Palermo</name></author><author><name sortKey="Boldrin, F" sort="Boldrin, F" uniqKey="Boldrin F" first="F" last="Boldrin">F. Boldrin</name></author><author><name sortKey="Sack, R" sort="Sack, R" uniqKey="Sack R" first="R" last="Sack">R. Sack</name></author><author><name sortKey="Hunziker, P" sort="Hunziker, P" uniqKey="Hunziker P" first="P" last="Hunziker">P. Hunziker</name></author><author><name sortKey="Piccinni, E L" sort="Piccinni, E L" uniqKey="Piccinni E" first="E L" last="Piccinni">E L Piccinni</name></author></analytic><series><title level="j">Protist</title><idno type="ISSN">1434-4610</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Copper (metabolism)</term><term>DNA, Complementary (MeSH)</term><term>DNA, Protozoan (MeSH)</term><term>Gene Expression (MeSH)</term><term>Metallothionein (genetics)</term><term>Metallothionein (isolation & purification)</term><term>Metallothionein (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Peptides (MeSH)</term><term>RNA, Messenger (MeSH)</term><term>Sequence Analysis, DNA (MeSH)</term><term>Sequence Analysis, Protein (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Tetrahymena (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Metallothionein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Metallothionein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term><term>Metallothionein</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Tetrahymena</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>DNA, Complementary</term><term>DNA, Protozoan</term><term>Gene Expression</term><term>Molecular Sequence Data</term><term>Peptides</term><term>RNA, Messenger</term><term>Sequence Analysis, DNA</term><term>Sequence Analysis, Protein</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The protist Tetrahymena pigmentosa accumulates large amounts of metal ions, particularly cadmium and copper. This capability is linked to the induction of metallothioneins (MTs), cysteine-rich metal-binding proteins found in protists, plants and animals. The present study focuses on a novel inducible MT-isoform isolated from Tetrahymena after exposure to a non-toxic dose of copper. The cDNA sequence was determined utilising the partial peptide sequence of purified protein. The Cu-MT cDNA encodes 96 amino acids containing 28 cysteine residues (29%) arranged in motifs characteristic of the metal-binding regions of vertebrate and invertebrate MTs. Both the amino acid and nucleotide sequences differ, not only from other animal MTs, but also from the previously characterised Tetrahymena Cd-MT. Both MTs contain the structural pattern GTXXXCKCXXCKC, which may be proposed as a conservative sequence of Tetrahymena MTs. Cu-dependent regulation of MT expression was also investigated by measuring MT-mRNA and MT levels. MT synthesis occurs very quickly and MT contents increase with Cu accumulation. The induction of Cu-MT mRNA is very rapid, with no observable lag period, and is characterised by transient fluctuation, similar to that described for Cd-MT mRNA. The data reported here indicate that, also in the unicellular organism Tetrahymena, two very different MT isoforms, which perform different biological functions, are expressed according to the inducing metal, Cu or Cd.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11693660</PMID><DateCompleted><Year>2002</Year><Month>05</Month><Day>07</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>05</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1434-4610</ISSN><JournalIssue CitedMedium="Print"><Volume>152</Volume><Issue>3</Issue><PubDate><Year>2001</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Protist</Title><ISOAbbreviation>Protist</ISOAbbreviation></Journal><ArticleTitle>Identification, cloning and characterisation of a novel copper-metallothionein in tetrahymena pigmentosa. Sequencing of cDNA and expression.</ArticleTitle><Pagination><MedlinePgn>219-29</MedlinePgn></Pagination><Abstract><AbstractText>The protist Tetrahymena pigmentosa accumulates large amounts of metal ions, particularly cadmium and copper. This capability is linked to the induction of metallothioneins (MTs), cysteine-rich metal-binding proteins found in protists, plants and animals. The present study focuses on a novel inducible MT-isoform isolated from Tetrahymena after exposure to a non-toxic dose of copper. The cDNA sequence was determined utilising the partial peptide sequence of purified protein. The Cu-MT cDNA encodes 96 amino acids containing 28 cysteine residues (29%) arranged in motifs characteristic of the metal-binding regions of vertebrate and invertebrate MTs. Both the amino acid and nucleotide sequences differ, not only from other animal MTs, but also from the previously characterised Tetrahymena Cd-MT. Both MTs contain the structural pattern GTXXXCKCXXCKC, which may be proposed as a conservative sequence of Tetrahymena MTs. Cu-dependent regulation of MT expression was also investigated by measuring MT-mRNA and MT levels. MT synthesis occurs very quickly and MT contents increase with Cu accumulation. The induction of Cu-MT mRNA is very rapid, with no observable lag period, and is characterised by transient fluctuation, similar to that described for Cd-MT mRNA. The data reported here indicate that, also in the unicellular organism Tetrahymena, two very different MT isoforms, which perform different biological functions, are expressed according to the inducing metal, Cu or Cd.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Santovito</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Padova, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Irato</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Palermo</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Boldrin</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Sack</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Hunziker</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author 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Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016054" MajorTopicYN="N">DNA, Protozoan</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="Y">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008668" MajorTopicYN="N">Metallothionein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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