Molecular and functional properties of an archaeal phenylalanyl-tRNA synthetase from the hyperthermophile Sulfolobus solfataricus.
An archaeal phenylalanyl-tRNA synthetase (FRS) has been purified from the hyperthermophile Sulfolobus solfataricus (Ss). This enzyme is a heterotetramer made of two different subunits whose molecular mass is 56 kDa and 64 kDa, respectively. As thought, SsFRS is essential for the in vitro poly(Phe) synthesis. Interestingly, the enzyme is able to aminoacylate only endogenous tRNA but it does not seem to be a strictly ATP-dependent synthetase. SsFRS interacts with the elongation factor 1alpha isolated from the same source; this caused a significant enhancement of the SstRNA aminoacylation efficiency, thus indicating that, as well as in eukarya, in this archaeon a tRNA channelling mechanism should occur. The overall results presented in this paper show that the archaeal SsFRS behaves as the analogous enzymes isolated from eukaryal sources rather than those from eubacterial organisms.
Lombardo
Barbara
B
Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II, Via S. Pansini, 5, I-80131, Naples, Italy.
Raimo
Gennaro
G
Bocchini
Vincenzo
V
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000595:Amino Acid Sequence; D004795:Enzyme Stability; D006160:Guanosine Triphosphate / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D020648:Peptide Elongation Factor 1 / Q000494:pharmacology; D010649:Phenylalanine / Q000737:chemistry; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology*; D013696:Temperature; D014316:Tritium
D020648:Peptide Elongation Factor 1; D014316:Tritium; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D010652:Phenylalanine-tRNA Ligase