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The A26G replacement in the consensus sequence A‐X‐X‐X‐X‐G‐K‐[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus

De Vendittis, Emmanuele ; Adinolfi, Bianca Stella ; Amatruda, Maria Rosa ; Raimo, Gennaro ; Masullo, Mariorosario ; Bocchini, Vincenzo

European journal of biochemistry, 1999-06, Vol.262 (2), p.600-605 [Periódico revisado por pares]

Oxford, UK: Blackwell Science Ltd

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Título:
The A26G replacement in the consensus sequence A‐X‐X‐X‐X‐G‐K‐[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus
Autor: De Vendittis, Emmanuele ; Adinolfi, Bianca Stella ; Amatruda, Maria Rosa ; Raimo, Gennaro ; Masullo, Mariorosario ; Bocchini, Vincenzo
Assuntos: archaeal elongation factor 2 ; Base Sequence ; Binding Sites ; Consensus Sequence ; DNA Primers ; elongation factor EF-2 ; Enzyme Activation ; ethylene glycol ; GTP Phosphohydrolase-Linked Elongation Factors - metabolism ; guanine nucleotide-binding protein ; Guanine Nucleotides - metabolism ; increased intrinsic GTPase ; Mutagenesis, Site-Directed ; mutant elongation factor 2 ; mutation in the GTP‐binding motif ; Peptide Elongation Factor 2 ; Peptide Elongation Factors - chemistry ; Peptide Elongation Factors - metabolism ; Sulfolobus - enzymology ; Sulfolobus - metabolism ; Sulfolobus solfataricus
É parte de: European journal of biochemistry, 1999-06, Vol.262 (2), p.600-605
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
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Descrição: A recombinant form of the elongation factor 2 from the archaeon Sulfolobus solfataricus (SsEF‐2), carrying the A26G substitution, has been produced and characterized. The amino acid replacement converted the guanine nucleotide binding consensus sequences A‐X‐X‐X‐X‐G‐K‐[T,S] of the elongation factors EF‐G or EF‐2 into the corresponding G‐X‐X‐X‐X‐G‐K‐[T,S] motif which is present in all the other GTP‐binding proteins. The rate of poly(U)‐directed poly(Phe) synthesis and the ribosome‐dependent GTPase activity of A26GSsEF‐2 were decreased compared to SsEF‐2, thus indicating that the A26G replacement partially affected the function of SsEF‐2 during translocation. In contrast, the A26G substitution enhanced the catalytic efficiency of the intrinsic SsEF‐2 GTPase triggered by ethylene glycol [Raimo, G., Masullo, M., Scarano, G., & Bocchini, V. (1997) Biochimie78, 832–837]. Surprisingly, A26GSsEF‐2 was able to hydrolyse GTP even in the absence of ethylene glycol; furthermore, the alcohol increased the affinity for GTP without modifying the catalytic constant of A26GSsEF‐2 GTPase. Compared to SsEF‐2, the affinity of A26GSsEF‐2 for [3H]GDP was significantly reduced. These findings suggest that A26 is a regulator of the biochemical functions of SsEF‐2. The involvement of this alanine residue in the guanine nucleotide‐binding pocket of EF‐2 or EF‐G is discussed.
Editor: Oxford, UK: Blackwell Science Ltd
Idioma: Inglês

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The A26G replacement in the consensus sequence A‐X‐X‐X‐X‐G‐K‐[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus

De Vendittis, Emmanuele ; Adinolfi, Bianca Stella ; Amatruda, Maria Rosa ; Raimo, Gennaro ; Masullo, Mariorosario ; Bocchini, Vincenzo

Oxford, UK: Blackwell Science Ltd

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