TY - JOUR
T1 - Protein synthesis in rabbit reticulocytes XXII
T2 - A heat stable dialyzable factor (EIF-1*) modulates Met-tRNAf binding to EIF-1
AU - Dasgupta, A.
AU - Roy, R.
AU - Palmieri, S.
AU - Das, A.
AU - Ralston, R.
AU - Gupta, N. K.
N1 - Funding Information:
of low molecular in reticulocyte first reported as an stable (22). The polyamines was also in this paper have described by'these establish that EIF-l* Acknowledgements This research was supported by NIH Research 22079. The authors thank Mr. Dennis Jurgens for locyte ribosomes and ribosomal salt wash.
PY - 1978/6/14
Y1 - 1978/6/14
N2 - The peptide chain initiation factor EIF-1 forms a ternary complex, Met-tRNAf·EIF-1·GTP in the absence of Mg++ and the preformed complex is stable to Mg++. However, with homogeneous preparations of EIF-1, addition of Mg++ during the initial formation of the ternary complex strongly inhibits the complex formation. A heat stable dialyzable factor (EIF-1*) which mostly remains associated with the high molecular weight protein complex, EIF-2 (TDF) during purification of the peptide chain initiation factors, has been purified using a phenol extraction procedure. EIF-1* restores the Met-tRNAf binding activity of EIF-1 in the presence of 1 mM Mg++; in the presence of EIF-1*, Met-tRNAf binding by EIF-1 shows a sharp Mg++ optimum around 1 mM. EIF-1* is heat stable, alkali stable, dialyzable and pronase sensitive. The same EIF-1* preparation also strongly inhibits Met-tRNAf binding to EIF-1 in the absence of Mg++ and stimulates protein synthesis in a mRNA-dependent rabbit reticulocyte lysate system.
AB - The peptide chain initiation factor EIF-1 forms a ternary complex, Met-tRNAf·EIF-1·GTP in the absence of Mg++ and the preformed complex is stable to Mg++. However, with homogeneous preparations of EIF-1, addition of Mg++ during the initial formation of the ternary complex strongly inhibits the complex formation. A heat stable dialyzable factor (EIF-1*) which mostly remains associated with the high molecular weight protein complex, EIF-2 (TDF) during purification of the peptide chain initiation factors, has been purified using a phenol extraction procedure. EIF-1* restores the Met-tRNAf binding activity of EIF-1 in the presence of 1 mM Mg++; in the presence of EIF-1*, Met-tRNAf binding by EIF-1 shows a sharp Mg++ optimum around 1 mM. EIF-1* is heat stable, alkali stable, dialyzable and pronase sensitive. The same EIF-1* preparation also strongly inhibits Met-tRNAf binding to EIF-1 in the absence of Mg++ and stimulates protein synthesis in a mRNA-dependent rabbit reticulocyte lysate system.
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U2 - 10.1016/0006-291X(78)90885-9
DO - 10.1016/0006-291X(78)90885-9
M3 - Article
C2 - 250438
AN - SCOPUS:0018192020
SN - 0006-291X
VL - 82
SP - 1019
EP - 1027
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -