Isolation and sequencing of a new β-galactosidase-encoding archaebacterial gene
Identifieur interne : 001F55 ( Istex/Checkpoint ); précédent : 001F54; suivant : 001F56Isolation and sequencing of a new β-galactosidase-encoding archaebacterial gene
Auteurs : Maria Vittoria Cubellis ; Carla Rozzo ; Piercarlo Montecucchi ; Mosè RossiSource :
- Gene [ 0378-1119 ] ; 1990.
English descriptors
- Teeft :
- Academic press, Archaebacterial, Archaebacterial genes, Archaebacterial promoters, Archaebacterium, Archaebacterium methanococcus voltae, Average size, Biochimica delle proteine, Clone, Codon, Codon preferences, Consensus sequence, Gene, Genes coding, Genes encoding, Genomic library, Good agreement, Lac, Lacs gene, Nucleic, Nucleic acids, Oligo probe, Positive clones, Primary structure, Promoter, Reeve, Reiter, Second library, Solfataricus, Solfataricus genome, Transcription initiation, Woese.
Abstract
Abstract: The gene lacS coding for a β-galactosidase (βGal; EC 3.2.1.23) has been cloned from the thermoacidophilic archaebacterium Sulfolobus solfataricus, strain MT-4. It encodes a polypeptide chain of 489 amino acids (aa) (56764 Da) in good agreement with the value directly measured for the enzyme (60 ± 2 kDa per subunit). The aa composition of the enzyme and, in particular, its peculiarly low cysteine content (one Cys per subunit) has been confirmed; at the same time, it has been observed that the very low G + C content of the S. solfataricus genome strongly influences the codoon usage preferences in the lacS sequence. There appears to be no evident similarity between this and the Escherichia coli lacZ sequence, thus suggesting that the two enzymes have analogous function, but are not homologous. By comparison with the published sequences of archaebacterial promoters, terminators and ribosome-binding sites, potential regulatory sites have been identified in the flanking regions of the S. solfataricus lacS gene.
Url:
DOI: 10.1016/0378-1119(90)90472-4
Affiliations:
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It encodes a polypeptide chain of 489 amino acids (aa) (56764 Da) in good agreement with the value directly measured for the enzyme (60 ± 2 kDa per subunit). The aa composition of the enzyme and, in particular, its peculiarly low cysteine content (one Cys per subunit) has been confirmed; at the same time, it has been observed that the very low G + C content of the S. solfataricus genome strongly influences the codoon usage preferences in the lacS sequence. There appears to be no evident similarity between this and the Escherichia coli lacZ sequence, thus suggesting that the two enzymes have analogous function, but are not homologous. By comparison with the published sequences of archaebacterial promoters, terminators and ribosome-binding sites, potential regulatory sites have been identified in the flanking regions of the S. solfataricus lacS gene.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Cubellis, Maria Vittoria" sort="Cubellis, Maria Vittoria" uniqKey="Cubellis M" first="Maria Vittoria" last="Cubellis">Maria Vittoria Cubellis</name><name sortKey="Montecucchi, Piercarlo" sort="Montecucchi, Piercarlo" uniqKey="Montecucchi P" first="Piercarlo" last="Montecucchi">Piercarlo Montecucchi</name><name sortKey="Rossi, Mose" sort="Rossi, Mose" uniqKey="Rossi M" first="Mosè" last="Rossi">Mosè Rossi</name><name sortKey="Rozzo, Carla" sort="Rozzo, Carla" uniqKey="Rozzo C" first="Carla" last="Rozzo">Carla Rozzo</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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