Periplasmic fractionation of Escherichia coli yields recombinant plastocyanin despite the absence of a signal sequence.
Identifieur interne : 004B25 ( Main/Exploration ); précédent : 004B24; suivant : 004B26Periplasmic fractionation of Escherichia coli yields recombinant plastocyanin despite the absence of a signal sequence.
Auteurs : J A Ybe [États-Unis] ; M H HechtSource :
- Protein expression and purification [ 1046-5928 ] ; 1994.
Descripteurs français
- KwdFr :
- Analyse de séquence (MeSH), Arbres (MeSH), Compartimentation cellulaire (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Fractionnement cellulaire (MeSH), Gènes de synthèse (génétique), Membrane cellulaire (composition chimique), Plastocyanine (biosynthèse), Plastocyanine (génétique), Plastocyanine (isolement et purification), Protéines recombinantes (biosynthèse), Protéines recombinantes (isolement et purification), Signaux de triage des protéines (génétique), Spectrophotométrie (MeSH), Spécificité d'espèce (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- biosynthèse : Plastocyanine, Protéines recombinantes.
- composition chimique : Membrane cellulaire.
- génétique : Escherichia coli, Gènes de synthèse, Plastocyanine, Signaux de triage des protéines.
- isolement et purification : Plastocyanine, Protéines recombinantes.
- Analyse de séquence, Arbres, Compartimentation cellulaire, Données de séquences moléculaires, Fractionnement cellulaire, Spectrophotométrie, Spécificité d'espèce, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cell Compartmentation (MeSH), Cell Fractionation (MeSH), Cell Membrane (chemistry), Escherichia coli (genetics), Genes, Synthetic (genetics), Molecular Sequence Data (MeSH), Plastocyanin (biosynthesis), Plastocyanin (genetics), Plastocyanin (isolation & purification), Protein Sorting Signals (genetics), Recombinant Proteins (biosynthesis), Recombinant Proteins (isolation & purification), Sequence Analysis (MeSH), Species Specificity (MeSH), Spectrophotometry (MeSH), Trees (MeSH).
- MESH :
- chemical , biosynthesis : Plastocyanin, Recombinant Proteins.
- chemistry : Cell Membrane.
- genetics : Escherichia coli, Genes, Synthetic, Plastocyanin, Protein Sorting Signals.
- chemical , isolation & purification : Plastocyanin, Recombinant Proteins.
- Amino Acid Sequence, Base Sequence, Cell Compartmentation, Cell Fractionation, Molecular Sequence Data, Sequence Analysis, Species Specificity, Spectrophotometry, Trees.
Abstract
Poplar plastocyanin has been expressed in E. coli from a synthetic gene cloned into the T7 expression system. Despite the absence of a signal sequence, large quantities of the recombinant protein were readily obtained by procedures typically used to isolate proteins from the bacterial periplasm. Several different fractionation methods were equally successful. The presence of plastocyanin in these fractions does not reflect wholesale leakage of intracellular proteins, since neither beta-galactosidase activity nor the bulk of Escherichia coli proteins were released by the fractionation. The identity of the overexpressed protein was unequivocally proven to be poplar plastocyanin by N-terminal amino acid sequence analysis and by spectroscopic characterization of the purified blue copper protein.
DOI: 10.1006/prep.1994.1047
PubMed: 7950377
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Ybe, J A" sort="Ybe, J A" uniqKey="Ybe J" first="J A" last="Ybe">J A Ybe</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry, Princeton University, New Jersey 08544-1009.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">New Jersey</region>
</placeName>
<wicri:cityArea>Department of Chemistry, Princeton University</wicri:cityArea>
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<author><name sortKey="Hecht, M H" sort="Hecht, M H" uniqKey="Hecht M" first="M H" last="Hecht">M H Hecht</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Cell Compartmentation (MeSH)</term>
<term>Cell Fractionation (MeSH)</term>
<term>Cell Membrane (chemistry)</term>
<term>Escherichia coli (genetics)</term>
<term>Genes, Synthetic (genetics)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Plastocyanin (biosynthesis)</term>
<term>Plastocyanin (genetics)</term>
<term>Plastocyanin (isolation & purification)</term>
<term>Protein Sorting Signals (genetics)</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Sequence Analysis (MeSH)</term>
<term>Species Specificity (MeSH)</term>
<term>Spectrophotometry (MeSH)</term>
<term>Trees (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence (MeSH)</term>
<term>Arbres (MeSH)</term>
<term>Compartimentation cellulaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Escherichia coli (génétique)</term>
<term>Fractionnement cellulaire (MeSH)</term>
<term>Gènes de synthèse (génétique)</term>
<term>Membrane cellulaire (composition chimique)</term>
<term>Plastocyanine (biosynthèse)</term>
<term>Plastocyanine (génétique)</term>
<term>Plastocyanine (isolement et purification)</term>
<term>Protéines recombinantes (biosynthèse)</term>
<term>Protéines recombinantes (isolement et purification)</term>
<term>Signaux de triage des protéines (génétique)</term>
<term>Spectrophotométrie (MeSH)</term>
<term>Spécificité d'espèce (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Plastocyanin</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Plastocyanine</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Membrane cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
<term>Genes, Synthetic</term>
<term>Plastocyanin</term>
<term>Protein Sorting Signals</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term>
<term>Gènes de synthèse</term>
<term>Plastocyanine</term>
<term>Signaux de triage des protéines</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Plastocyanin</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Plastocyanine</term>
<term>Protéines recombinantes</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Cell Compartmentation</term>
<term>Cell Fractionation</term>
<term>Molecular Sequence Data</term>
<term>Sequence Analysis</term>
<term>Species Specificity</term>
<term>Spectrophotometry</term>
<term>Trees</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence</term>
<term>Arbres</term>
<term>Compartimentation cellulaire</term>
<term>Données de séquences moléculaires</term>
<term>Fractionnement cellulaire</term>
<term>Spectrophotométrie</term>
<term>Spécificité d'espèce</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
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<front><div type="abstract" xml:lang="en">Poplar plastocyanin has been expressed in E. coli from a synthetic gene cloned into the T7 expression system. Despite the absence of a signal sequence, large quantities of the recombinant protein were readily obtained by procedures typically used to isolate proteins from the bacterial periplasm. Several different fractionation methods were equally successful. The presence of plastocyanin in these fractions does not reflect wholesale leakage of intracellular proteins, since neither beta-galactosidase activity nor the bulk of Escherichia coli proteins were released by the fractionation. The identity of the overexpressed protein was unequivocally proven to be poplar plastocyanin by N-terminal amino acid sequence analysis and by spectroscopic characterization of the purified blue copper protein.</div>
</front>
</TEI>
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<DateRevised><Year>2007</Year>
<Month>11</Month>
<Day>14</Day>
</DateRevised>
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<JournalIssue CitedMedium="Print"><Volume>5</Volume>
<Issue>4</Issue>
<PubDate><Year>1994</Year>
<Month>Aug</Month>
</PubDate>
</JournalIssue>
<Title>Protein expression and purification</Title>
<ISOAbbreviation>Protein Expr Purif</ISOAbbreviation>
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<ArticleTitle>Periplasmic fractionation of Escherichia coli yields recombinant plastocyanin despite the absence of a signal sequence.</ArticleTitle>
<Pagination><MedlinePgn>317-23</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Poplar plastocyanin has been expressed in E. coli from a synthetic gene cloned into the T7 expression system. Despite the absence of a signal sequence, large quantities of the recombinant protein were readily obtained by procedures typically used to isolate proteins from the bacterial periplasm. Several different fractionation methods were equally successful. The presence of plastocyanin in these fractions does not reflect wholesale leakage of intracellular proteins, since neither beta-galactosidase activity nor the bulk of Escherichia coli proteins were released by the fractionation. The identity of the overexpressed protein was unequivocally proven to be poplar plastocyanin by N-terminal amino acid sequence analysis and by spectroscopic characterization of the purified blue copper protein.</AbstractText>
</Abstract>
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