mRNA binding properties of wheat germ protein synthesis initiation factor 2.
The binding of protein synthesis initiation factor (eIF-) 2 to mRNA was measured by retention of the mRNA.eIF-2 complexes on nitrocellulose filters. The binding of eIF-2 to mRNA was inhibited by GDP and GTP; the inhibition by GTP was enhanced by the presence of Met-tRNA(i). In addition, the formation of eIF-2.GDP binary complex and eIF-2.GTP.Met-tRNA(i) ternary complex was inhibited by mRNA. These data indicate that mRNA binds to a site on eIF-2 that is the same or overlaps the site to which guanine nucleotides bind eIF-2. This finding strongly suggests that inhibition of ternary complex formation by mRNA may be the result of competition between mRNA and GTP and not competition between mRNA and Met-tRNA(i).
Benkowski
L A
LA
Department of Chemistry and Biochemistry, University of Texas, Austin 78712, USA.
Ravel
J M
JM
Browning
K S
KS
D004247:DNA / Q000494:pharmacology; D004277:DNA, Single-Stranded / Q000494:pharmacology; D015852:Eukaryotic Initiation Factor-2 / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D007700:Kinetics; D011061:Poly A / Q000494:pharmacology; D011072:Poly U / Q000494:pharmacology; D011485:Protein Binding; D012333:RNA, Messenger / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D012337:RNA, Ribosomal, 18S / Q000494:pharmacology; D012358:RNA, Transfer, Met / Q000378:metabolism; D012265:Ribonucleotides / Q000494:pharmacology; D012639:Seeds / Q000378:metabolism; D014908:Triticum / Q000378:metabolism*
D004277:DNA, Single-Stranded; D015852:Eukaryotic Initiation Factor-2; D012333:RNA, Messenger; D012337:RNA, Ribosomal, 18S; D012358:RNA, Transfer, Met; D012265:Ribonucleotides; D006153:Guanosine Diphosphate; D011061:Poly A; D011072:Poly U; D006160:Guanosine Triphosphate; D004247:DNA