Cloning and sequencing of the gene encoding thermostable elongation factor 2 in Sulfolobus solfataricus.
The gene (aEF-2) coding for the translation elongation factor 2 (aEF-2) in the thermoacidophilic archaebacterium, Sulfolobus solfataricus, has been cloned and sequenced. The deduced primary structure of aEF-2 is composed of 735 amino acids (aa), excluding the Met start residue. There are no Cys residues and the calculated M(r) is 81,699. In the coding region of aEF-2, the high A + T content greatly influences the codon usage. From the alignment of the primary structure of aEF-2 with that of the analogous factors from the three kingdoms, aa identities were derived. The greatest identity (82%) was found with EF-2 from Sulfolobus acidocaldarius; lower values were observed with other archaebacterial EF-2 (45-47%), eukaryotic EF-2 (38-40%) and with the functional eubacterial analogue EF-G (28-31%). aEF-2 possesses the consensus sequences required for a GTP-binding protein and the four regions which are supposed to be involved in the functional regulation of EF-2/EF-G. These data should have phylogenetic implications.
De Vendittis
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Dipartimento di Biochemica e Biotecnologie Mediche, Università di Napoli Federico II, Naples, Italy.
Amatruda
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MR
Masullo
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Bocchini
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D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003062:Codon; D004269:DNA, Bacterial; D005798:Genes, Bacterial; D006160:Guanosine Triphosphate / Q000378:metabolism; D006358:Hot Temperature; D008969:Molecular Sequence Data; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000235:genetics* / Q000378:metabolism; D012045:Regulatory Sequences, Nucleic Acid; D017386:Sequence Homology, Amino Acid; D016944:Sulfolobus / Q000235:genetics*
D003062:Codon; D004269:DNA, Bacterial; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D006160:Guanosine Triphosphate