The cloning and sequencing of the gene coding for the archaebacterial elongation factor 1α (aEF-1α) was performed by screening a Sulfolobus solfataricus genomic library using a probe constructed from the eptapeptide KNMITGA that is conserved in all the EF-1α / EF-Tu known so far. The isolated recombinant phage contained the part of the aEF-1α gene from amino acids 1 to 171. The other part (amino acids 162–435) was obtained through the amplification of the S. solfataricus DNA by PCR. The codon usage by the aEF-1α gene showed a preference for triplets ending in A and / or T. This behavior was almost identical to that of the S. acidocaldarius EF-1α gene but differed greatly from that of EF-1α / EF-Tu genes in other archaebacteria eukaryotes and eubacteria. The translated protein is made of 435 amino acid residues and contains sequence motifs for the binding of GTP, tRNA and ribosome. Alignments of aEF-1α with several EF-1α/EF-Tu revealed that aEF-1α is more similar to its eukaryotic than to its eubacterial counterparts.

The nucleotide sequence of the gene coding for the elongation factor 1α in Sulfolobus solfataricus. Homology of the product with related proteins

ARCARI, PAOLO;GALLO, MONICA;DELLO RUSSO, ANTONIO;
1994

Abstract

The cloning and sequencing of the gene coding for the archaebacterial elongation factor 1α (aEF-1α) was performed by screening a Sulfolobus solfataricus genomic library using a probe constructed from the eptapeptide KNMITGA that is conserved in all the EF-1α / EF-Tu known so far. The isolated recombinant phage contained the part of the aEF-1α gene from amino acids 1 to 171. The other part (amino acids 162–435) was obtained through the amplification of the S. solfataricus DNA by PCR. The codon usage by the aEF-1α gene showed a preference for triplets ending in A and / or T. This behavior was almost identical to that of the S. acidocaldarius EF-1α gene but differed greatly from that of EF-1α / EF-Tu genes in other archaebacteria eukaryotes and eubacteria. The translated protein is made of 435 amino acid residues and contains sequence motifs for the binding of GTP, tRNA and ribosome. Alignments of aEF-1α with several EF-1α/EF-Tu revealed that aEF-1α is more similar to its eukaryotic than to its eubacterial counterparts.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/592390
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