CTP can replace GTP in reactions catalyzed by eukaryotic peptide elongation factor 1

In several reactions catalyzed by highly purified peptide elongation factor 1 from rabbit reticulocytes, GTP may be fully replaced by CTP but not by ATP or UTP. This holds true for the factor-dependent binding of aminoacyl-tRNA to ribosomes, GTPase activity, GTP-dependent autophosphorylation of the...

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Veröffentlicht in:	FEBS letters 1984-11, Vol.177 (1), p.112-114
Hauptverfasser:	Tuháčková, Z., Havránek, M., Hradec, J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Autocatalytic phosphorylation Cholesteryl 14-methylhexadecanoate Biological and medical sciences CTP Cytidine Triphosphate - metabolism Cytosine Nucleotides - metabolism Fundamental and applied biological sciences. Psychology GTP GTPase Guanosine Triphosphate - metabolism Kinetics Molecular and cellular biology Molecular genetics Peptide Elongation Factor 1 Peptide Elongation Factors - metabolism Phosphates - metabolism Poly U - metabolism RNA, Transfer, Amino Acyl - metabolism Translation. Translation factors. Protein processing Uridine Triphosphate - metabolism
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Beschreibung
Zusammenfassung:	In several reactions catalyzed by highly purified peptide elongation factor 1 from rabbit reticulocytes, GTP may be fully replaced by CTP but not by ATP or UTP. This holds true for the factor-dependent binding of aminoacyl-tRNA to ribosomes, GTPase activity, GTP-dependent autophosphorylation of the factor protein and binding of cholesteryl 14-methylhexadecanoate by the factor.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(84)80992-8