Natural mRNA is required for directing Met-tRNAf binding to 40S ribosomal subunits in animal cells: involvement of Co-eIF-2A in natural mRNA-directed initiation complex formation

Biochemistry ◽  
1988 ◽  
Vol 27 (21) ◽  
pp. 8203-8209 ◽  
Author(s):  
Ananda L. Roy ◽  
Debopam Chakrabarti ◽  
Bansidhar Datta ◽  
Ronald E. Hileman ◽  
Naba K. Gupta
Keyword(s):  
Complex Formation ◽  
Animal Cells ◽  
Initiation Complex ◽  
Ribosomal Subunits

scholarly journals The Oxazolidinone Linezolid Inhibits Initiation of Protein Synthesis in Bacteria

1998 ◽  
Vol 42 (12) ◽  
pp. 3251-3255 ◽  
Author(s):  
Steve M. Swaney ◽  
Hiroyuki Aoki ◽  
M. Clelia Ganoza ◽  
Dean L. Shinabarger
Keyword(s):  
Protein Synthesis ◽  
Complex Formation ◽  
Antimicrobial Agents ◽  
Ribosomal Subunit ◽  
Multidrug Resistant ◽  
Binary Complex ◽  
Initiation Complex ◽  
Ribosomal Subunits ◽  
Bacterial Translation

ABSTRACT The oxazolidinones represent a new class of antimicrobial agents which are active against multidrug-resistant staphylococci, streptococci, and enterococci. Previous studies have demonstrated that oxazolidinones inhibit bacterial translation in vitro at a step preceding elongation but after the charging ofN-formylmethionine to the initiator tRNA molecule. The event that occurs between these two steps is termed initiation. Initiation of protein synthesis requires the simultaneous presence of N-formylmethionine-tRNA, the 30S ribosomal subunit, mRNA, GTP, and the initiation factors IF1, IF2, and IF3. An initiation complex assay measuring the binding of [3H]N-formylmethionyl-tRNA to ribosomes in response to mRNA binding was used in order to investigate the mechanism of oxazolidinone action. Linezolid inhibited initiation complex formation with either the 30S or the 70S ribosomal subunits fromEscherichia coli. In addition, complex formation withStaphylococcus aureus 70S tight-couple ribosomes was inhibited by linezolid. Linezolid did not inhibit the independent binding of either mRNA or N-formylmethionyl-tRNA toE. coli 30S ribosomal subunits, nor did it prevent the formation of the IF2–N-formylmethionyl-tRNA binary complex. The results demonstrate that oxazolidinones inhibit the formation of the initiation complex in bacterial translation systems by preventing formation of theN-formylmethionyl-tRNA–ribosome–mRNA ternary complex.

scholarly journals Early effects of dimethylnitrosamine on the initiation of protein synthesis in mouse liver

1981 ◽  
Vol 194 (2) ◽  
pp. 469-474
Author(s):  
O Nygård ◽  
T Hultin
Keyword(s):  
Protein Synthesis ◽  
Complex Formation ◽  
Intraperitoneal Injection ◽  
Mouse Liver ◽  
Initiation Complex ◽  
Ribosomal Subunits ◽  
Single Intraperitoneal Injection ◽  
System 2 ◽  
Early Effects ◽  
Ribosomal Complex

1. Dimethylnitrosamine (37.5 mg/kg body wt.) was administered to mice by a single intraperitoneal injection, and the early effects on protein synthesis and related functions were studied in a liver S-30 system. 2. The incorporation of [14C]leucine into protein decreased rapidly after dimethylnitrosamine administration. The effect was associated with a decreased ability of the system to utilize methionyl-tRNAfMet and formyl-methionyl-tRNAfMet for 80 S ribosomal initiation-complex formation (primary initiation), and a loss of poly(A)-containing RNA from the postmicrosomal fraction. All the three effects developed simultaneously, and were clearly demonstrable within 15 min. 3. Initiation-complex formation in the polyribosomal fraction (re-initiation) was decreased to the same extent as the primary initiation, indicating that the initiation defect was not a result of the decrease in free mRNA. 4. The inhibition of initiation was only manifest at the joining of the 40 S pre-initiation complex to 60 S ribosomal subunits. It was not a result of methionyl-tRNAfMet deacylation. The functions between the formation of the methionyl-tRNAfMet-containing 80 S ribosomal complex and the first translocation on the ribosome were not involved, since the incorporation of formylmethionine into N-terminal polypeptides decreased to the same extent as the 80 S initiation-complex formation. 5. Inhibitors of protein synthesis (cycloheximide and pactamycin) decreased poly(A)-containing RNA in the postmicrosomal fraction in a similar way to dimethylnitrosamine.

scholarly journals Eukaryotic initiation complex formation. Evidence for two distinct pathways

1975 ◽  
Vol 250 (23) ◽  
pp. 9083-9089
Author(s):  
SL Adams ◽  
B Safer ◽  
WF Anderson ◽  
WC Merrick
Keyword(s):  
Complex Formation ◽  
Initiation Complex

scholarly journals Differential requirement of a distal regulatory region for pre-initiation complex formation at globin gene promoters

2009 ◽  
Vol 37 (16) ◽  
pp. 5295-5308 ◽  
Author(s):  
Julie Ross ◽  
Stefania Bottardi ◽  
Vincent Bourgoin ◽  
Alex Wollenschlaeger ◽  
Elliot Drobetsky ◽  
...  
Keyword(s):  
Complex Formation ◽  
Globin Gene ◽  
Regulatory Region ◽  
Gene Promoters ◽  
Initiation Complex ◽  
Distal Regulatory Region
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