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Expression in Escherichia coli of the gene encoding thermostable elongation factor 2 in the archaebacterium Sulfolobus solfataricus
No full textHeterologous expression in Escherichia coli of the gene encoding an archaeal thermoacidophilic elongation factor 2. Properties of the recombinant protein
No full textExpression in Escherichia coli of the gene encoding thermostable elongation factor 2 in the archaebacterium Sulfolobus solfataricus
No full textCloning and sequencing of the gene encoding thermostable elongation factor 2 in Sulfolobus solfataricus
No full textEffect of the Gly82-->Ser substitution on the interaction of the yeast Ras2 protein with guanine nucleotides
No full textEffect of the Gly82-->Ser substitution on the interaction of the yeast Ras2 protein with guanine nucleotides
No full textHeterologous expression in Escherichia coli of the gene encoding an archaeal thermoacidophilic elongation factor 2. Properties of the recombinant protein
No full textCloning and sequencing of the gene encoding thermostable elongation factor 2 in Sulfolobus solfataricus
No full textThe A26G replacement in the consensus sequence AXXXXGK[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus
No full textCloning and sequencing of the gene encoding thermostable elongation factor 2 in Sulfolobus solfataricus
No full textThe 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
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