Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes.
Identifieur interne : 001119 ( Main/Exploration ); précédent : 001118; suivant : 001120Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes.
Auteurs : H. Lüdemann [Allemagne] ; M. Dormeyer ; C. Sticherling ; D. Stallmann ; H. Follmann ; R L Krauth-SiegelSource :
- FEBS letters [ 0014-5793 ] ; 1998.
Descripteurs français
- KwdFr :
- ADN complémentaire (MeSH), Animaux (MeSH), Catalyse (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Trypanosoma brucei brucei (composition chimique).
- MESH :
- composition chimique : Thiorédoxines, Trypanosoma brucei brucei.
- génétique : Escherichia coli, Protéines recombinantes, Thiorédoxines.
- métabolisme : Protéines recombinantes, Thiorédoxines.
- ADN complémentaire, Animaux, Catalyse, Clonage moléculaire, Données de séquences moléculaires, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Catalysis (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (MeSH), Escherichia coli (genetics), Molecular Sequence Data (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (metabolism), Trypanosoma brucei brucei (chemistry).
- MESH :
- chemical , chemistry : Thioredoxins.
- chemical , genetics : Recombinant Proteins, Thioredoxins.
- chemical , metabolism : Recombinant Proteins, Thioredoxins.
- chemical : DNA, Complementary.
- chemistry : Trypanosoma brucei brucei.
- genetics : Escherichia coli.
- Amino Acid Sequence, Animals, Base Sequence, Catalysis, Cloning, Molecular, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
A gene has been cloned from Trypanosoma brucei which encodes a protein of 144 amino acid residues containing the thioredoxin-like motif WCPPCR. Overexpression of the gene in E. coli resulted in 4 mg pure protein from 100 ml bacterial cell culture. Recombinant T. brucei tryparedoxin acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione. This dithiol, exclusively found in parasitic protozoa, also reduces E. coli glutaredoxin but not thioredoxin. The trypanothione/tryparedoxin couple is an effective reductant of T. brucei ribonucleotide reductase. Like thioredoxins it has a poor GSH:disulfide transhydrogenase activity. The catalytic properties of tryparedoxin are intermediate between those of classical thioredoxins and glutaredoxins which indicates that these parasite proteins may form a new class of thiol-disulfide oxidoreductases.
DOI: 10.1016/s0014-5793(98)00793-5
PubMed: 9714547
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Dormeyer</name></author><author><name sortKey="Sticherling, C" sort="Sticherling, C" uniqKey="Sticherling C" first="C" last="Sticherling">C. Sticherling</name></author><author><name sortKey="Stallmann, D" sort="Stallmann, D" uniqKey="Stallmann D" first="D" last="Stallmann">D. Stallmann</name></author><author><name sortKey="Follmann, H" sort="Follmann, H" uniqKey="Follmann H" first="H" last="Follmann">H. 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Stallmann</name></author><author><name sortKey="Follmann, H" sort="Follmann, H" uniqKey="Follmann H" first="H" last="Follmann">H. Follmann</name></author><author><name sortKey="Krauth Siegel, R L" sort="Krauth Siegel, R L" uniqKey="Krauth Siegel R" first="R L" last="Krauth-Siegel">R L Krauth-Siegel</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1998" type="published">1998</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>Catalysis (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (MeSH)</term><term>Escherichia coli (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term><term>Trypanosoma brucei brucei (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (MeSH)</term><term>Animaux (MeSH)</term><term>Catalyse (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (génétique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term><term>Trypanosoma brucei brucei (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA, Complementary</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Thiorédoxines</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Catalysis</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN complémentaire</term><term>Animaux</term><term>Catalyse</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A gene has been cloned from Trypanosoma brucei which encodes a protein of 144 amino acid residues containing the thioredoxin-like motif WCPPCR. Overexpression of the gene in E. coli resulted in 4 mg pure protein from 100 ml bacterial cell culture. Recombinant T. brucei tryparedoxin acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione. This dithiol, exclusively found in parasitic protozoa, also reduces E. coli glutaredoxin but not thioredoxin. The trypanothione/tryparedoxin couple is an effective reductant of T. brucei ribonucleotide reductase. Like thioredoxins it has a poor GSH:disulfide transhydrogenase activity. The catalytic properties of tryparedoxin are intermediate between those of classical thioredoxins and glutaredoxins which indicates that these parasite proteins may form a new class of thiol-disulfide oxidoreductases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9714547</PMID><DateCompleted><Year>1998</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>431</Volume><Issue>3</Issue><PubDate><Year>1998</Year><Month>Jul</Month><Day>24</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes.</ArticleTitle><Pagination><MedlinePgn>381-5</MedlinePgn></Pagination><Abstract><AbstractText>A gene has been cloned from Trypanosoma brucei which encodes a protein of 144 amino acid residues containing the thioredoxin-like motif WCPPCR. Overexpression of the gene in E. coli resulted in 4 mg pure protein from 100 ml bacterial cell culture. Recombinant T. brucei tryparedoxin acts as a thiol-disulfide oxidoreductase. It is spontaneously reduced by trypanothione. This dithiol, exclusively found in parasitic protozoa, also reduces E. coli glutaredoxin but not thioredoxin. The trypanothione/tryparedoxin couple is an effective reductant of T. brucei ribonucleotide reductase. Like thioredoxins it has a poor GSH:disulfide transhydrogenase activity. The catalytic properties of tryparedoxin are intermediate between those of classical thioredoxins and glutaredoxins which indicates that these parasite proteins may form a new class of thiol-disulfide oxidoreductases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lüdemann</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Biochimie-Zentrum Heidelberg, Ruprecht-Karls-Universität, Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dormeyer</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Sticherling</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Stallmann</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Follmann</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Krauth-Siegel</LastName><ForeName>R L</ForeName><Initials>RL</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AJ006403</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C114110">tryparedoxin</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>FEBS Lett 1998 Oct 16;437(1-2):165</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014346" MajorTopicYN="N">Trypanosoma brucei brucei</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>8</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>8</Month><Day>26</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>8</Month><Day>26</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9714547</ArticleId><ArticleId IdType="pii">S0014-5793(98)00793-5</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(98)00793-5</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li></region><settlement><li>Heidelberg</li></settlement></list><tree><noCountry><name sortKey="Dormeyer, M" sort="Dormeyer, M" uniqKey="Dormeyer M" first="M" last="Dormeyer">M. Dormeyer</name><name sortKey="Follmann, H" sort="Follmann, H" uniqKey="Follmann H" first="H" last="Follmann">H. Follmann</name><name sortKey="Krauth Siegel, R L" sort="Krauth Siegel, R L" uniqKey="Krauth Siegel R" first="R L" last="Krauth-Siegel">R L Krauth-Siegel</name><name sortKey="Stallmann, D" sort="Stallmann, D" uniqKey="Stallmann D" first="D" last="Stallmann">D. Stallmann</name><name sortKey="Sticherling, C" sort="Sticherling, C" uniqKey="Sticherling C" first="C" last="Sticherling">C. Sticherling</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Ludemann, H" sort="Ludemann, H" uniqKey="Ludemann H" first="H" last="Lüdemann">H. Lüdemann</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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