scholarly journals Differential requirements for polypeptide chain initiation complex formation at the three bacteriophage R17 initiator regions

1977 ◽  
Vol 4 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Joan Argetsinger Steitz ◽  
Albert J. Wahba ◽  
Michael Laughrea ◽  
Peter B. Moore
Keyword(s):  
Complex Formation ◽  
Polypeptide Chain ◽  
Initiation Complex ◽  
Chain Initiation

Hypoxanthine-xanthine oxidase-related defect in polypeptide chain initiation by endothelium

1989 ◽  
Vol 66 (1) ◽  
pp. 450-457 ◽  
Author(s):  
L. Jornot ◽  
A. F. Junod
Keyword(s):  
Protein Synthesis ◽  
Xanthine Oxidase ◽  
Rna Synthesis ◽  
Polypeptide Chain ◽  
Total Proteins ◽  
Initiation Complex ◽  
Chain Initiation ◽  
Oxidase System ◽  
Initiation Factors ◽  
Related Defect

After exposure to O2 intermediates generated by the hypoxanthine-xanthine oxidase system (HX-XO), the rate of [3H]phenylalanine incorporation into total proteins in cultured endothelial cells was markedly reduced. This reduction, which was prevented by catalase, could not be explained by 1) changes in amino acid pools, 2) increased rate of degradation of newly synthesized proteins, 3) impaired poly(A)+ RNA synthesis and efficiency, 4) decreased rate of amino acylation. On the other hand, the increase in the monoribosome-to-polyribosome ratio suggested that translation was affected at the level of chain initiation. Further analysis indicated that 40S initiation complex formation was normal, whereas the assembly of 80S initiation complex was inhibited. Results from reconstitution experiments showed that both normal and treated ribosomes could support normal protein synthesis in the presence of normal initiation factors (IFs). In contrast, IFs from HX-XO lysates did not support normal protein synthesis with ribosomes from either source. Thus, the effect of XO treatment on protein synthesis appears to be an initiation defect related to decreased IF activity and/or availability.

scholarly journals Lack of inhibition by l-1-chloro-4-phenyl-3-toluene-p-sulphoamidobutan-2-one (l-1-tosylamido-2-phenylethyl chloromethyl ketone) of the formation of bacterial polypeptide chain initiation complex (Short Communication)

1973 ◽  
Vol 136 (2) ◽  
pp. 433-436 ◽  
Author(s):  
J. Jonák ◽  
B. F. C. Clark
Keyword(s):  
Short Communication ◽  
Polypeptide Chain ◽  
Protein Biosynthesis ◽  
Elongation Factor ◽  
Initiation Factor ◽  
Chain Elongation ◽  
Initiation Complex ◽  
Chloromethyl Ketone ◽  
Chain Initiation

The chymotrypsin inhibitor l-1-chloro-4-phenyl-3-toluene-p-sulphonamidobutan-2-one does not inhibit the function of the initiation factor during the formation of the polypeptide chain initiation complex in vitro. Since the inhibitor has been shown previously to inhibit polypeptide chain elongation by reacting with elongation factor EF-Tu, the inhibitor can be used to investigate the initiation and elongation steps of protein biosynthesis separately.

scholarly journals Polypeptide chain initiation in eukaryotes: mechanism of formation of initiation complex.

1976 ◽  
Vol 73 (2) ◽  
pp. 298-301 ◽  
Author(s):  
C. Nombela ◽  
N. A. Nombela ◽  
S. Ochoa ◽  
B. Safer ◽  
W. F. Anderson ◽  
...  
Keyword(s):  
Polypeptide Chain ◽  
Mechanism Of Formation ◽  
Initiation Complex ◽  
Chain Initiation
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