Amino terminal sequence of the mitochondrial protein mtDBP-C: similarity with nonhistone chromosomal proteins HMG 1 and 2.
Identifieur interne : 000042 ( Main/Exploration ); précédent : 000041; suivant : 000043Amino terminal sequence of the mitochondrial protein mtDBP-C: similarity with nonhistone chromosomal proteins HMG 1 and 2.
Auteurs : R. Ghrir [Tunisie] ; B. Mignotte ; M. GuérideSource :
- Biochimie [ 0300-9084 ] ; 1991.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Données de séquences moléculaires (MeSH), Femelle (MeSH), Protéines HMG (composition chimique), Protéines de Xénope (MeSH), Protéines de liaison à l'ADN (composition chimique), Similitude de séquences d'acides nucléiques (MeSH), Séquence d'acides aminés (MeSH), Xenopus laevis (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
Abstract
We have previously reported the characterization of a DNA-binding protein isolated from Xenopus laevis mitochondria (mtDBP-C). The amino terminal sequence of this protein (26 residues) has been determined by automated Edman degradation and used to search for sequence similarity with the NBRF library. A segment of 17 amino acids displays 47.1% of identity with proteins HMG-1 and 2 of various vertebrate species.
DOI: 10.1016/0300-9084(91)90031-u
PubMed: 1764507
Affiliations:
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- to stream PubMed, to step Curation: 000833
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- to stream Main, to step Curation: 000042
Le document en format XML
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<author><name sortKey="Gueride, M" sort="Gueride, M" uniqKey="Gueride M" first="M" last="Guéride">M. Guéride</name>
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<series><title level="j">Biochimie</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Animals (MeSH)</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>Female (MeSH)</term>
<term>High Mobility Group Proteins (chemistry)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Sequence Homology, Nucleic Acid (MeSH)</term>
<term>Xenopus Proteins (MeSH)</term>
<term>Xenopus laevis (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Femelle (MeSH)</term>
<term>Protéines HMG (composition chimique)</term>
<term>Protéines de Xénope (MeSH)</term>
<term>Protéines de liaison à l'ADN (composition chimique)</term>
<term>Similitude de séquences d'acides nucléiques (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Xenopus laevis (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA-Binding Proteins</term>
<term>High Mobility Group Proteins</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines HMG</term>
<term>Protéines de liaison à l'ADN</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Female</term>
<term>Molecular Sequence Data</term>
<term>Sequence Homology, Nucleic Acid</term>
<term>Xenopus Proteins</term>
<term>Xenopus laevis</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Données de séquences moléculaires</term>
<term>Femelle</term>
<term>Protéines de Xénope</term>
<term>Similitude de séquences d'acides nucléiques</term>
<term>Séquence d'acides aminés</term>
<term>Xenopus laevis</term>
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<front><div type="abstract" xml:lang="en">We have previously reported the characterization of a DNA-binding protein isolated from Xenopus laevis mitochondria (mtDBP-C). The amino terminal sequence of this protein (26 residues) has been determined by automated Edman degradation and used to search for sequence similarity with the NBRF library. A segment of 17 amino acids displays 47.1% of identity with proteins HMG-1 and 2 of various vertebrate species.</div>
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<country name="Tunisie"><noRegion><name sortKey="Ghrir, R" sort="Ghrir, R" uniqKey="Ghrir R" first="R" last="Ghrir">R. Ghrir</name>
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