Title : Formation and release of eukaryotic initiation factor 2 X GDP complex during eukaryotic ribosomal polypeptide chain initiation complex formation.

Pub. Date : 1985 Feb 25

PMID : 3844406






5 Functional Relationships(s)
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1 The formation and release of an eukaryotic initiation factor (eIF)-2 X GDP binary complex during eIF-5-mediated assembly of an 80 S ribosomal polypeptide chain initiation complex have been studied by sucrose gradient centrifugation analysis. Guanosine Diphosphate eukaryotic translation initiation factor 5 Homo sapiens
2 Isolated 40 S initiation complex reacts with eIF-5 and 60 S ribosomal subunits to form an 80 S ribosomal initiation complex with concomitant hydrolysis of an equimolar amount of bound GTP to GDP and Pi. Guanosine Diphosphate eukaryotic translation initiation factor 5 Homo sapiens
3 Evidence is presented that eIF-5-mediated hydrolysis releases the GTP bound to the 40 S initiation complex as an intact eIF-2 X GDP complex rather than as free GDP and eIF-2 which subsequently recombine to form the binary complex. Guanosine Diphosphate eukaryotic translation initiation factor 5 Homo sapiens
4 Evidence is presented that eIF-5-mediated hydrolysis releases the GTP bound to the 40 S initiation complex as an intact eIF-2 X GDP complex rather than as free GDP and eIF-2 which subsequently recombine to form the binary complex. Guanosine Diphosphate eukaryotic translation initiation factor 5 Homo sapiens
5 Furthermore, formation and release of eIF-2 X GDP from the ribosomal complex do not require concomitant formation of an 80 S initiation complex since both reactions occur efficiently when the 40 S initiation complex reacts with eIF-5 in the absence of 60 S ribosomal subunits. Guanosine Diphosphate eukaryotic translation initiation factor 5 Homo sapiens