Peptide chain elongation. Role of the S1 factor in the pathway form S3-guanosine diphosphate complex to aminoacyl transfer ribonucleic acid-S3-guanosine triphosphate complex

Biochemistry ◽  
1971 ◽  
Vol 10 (26) ◽  
pp. 4899-4906 ◽  
Author(s):  
Georges Beaud ◽  
Peter Lengyel
Keyword(s):  
Ribonucleic Acid ◽  
Peptide Chain ◽  
Chain Elongation ◽  
Guanosine Triphosphate ◽  
Guanosine Diphosphate ◽  
Aminoacyl Transfer

scholarly journals The Role of Guanosine Triphosphate Hydrolysis in Elongation Factor Tu-promoted Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes

1973 ◽  
Vol 248 (1) ◽  
pp. 375-377 ◽  
Author(s):  
Hideyoshi Yokosawa ◽  
Noriko Inoue-Yokosawa ◽  
Ken-Ichi Arai ◽  
Masao Kawakita ◽  
Yoshito Kaziro
Keyword(s):  
Ribonucleic Acid ◽  
Elongation Factor ◽  
Elongation Factor Tu ◽  
Guanosine Triphosphate ◽  
Aminoacyl Transfer

scholarly journals The Membrane Dynamics of Pexophagy Are Influenced by Sar1p in Pichia pastoris

2008 ◽  
Vol 19 (11) ◽  
pp. 4888-4899 ◽  
Author(s):  
Laura A. Schroder ◽  
Michael V. Ortiz ◽  
William A. Dunn
Keyword(s):  
Pichia Pastoris ◽  
Membrane Dynamics ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Wild Type ◽  
Guanosine Triphosphate ◽  
Guanosine Diphosphate ◽  
Mutant Forms ◽  
Negative Mutant

Several Sec proteins including a guanosine diphosphate/guanosine triphosphate exchange factor for Sar1p have been implicated in autophagy. In this study, we investigated the role of Sar1p in pexophagy by expressing dominant-negative mutant forms of Sar1p in Pichia pastoris. When expressing sar1pT34N or sar1pH79G, starvation-induced autophagy, glucose-induced micropexophagy, and ethanol-induced macropexophagy are dramatically suppressed. These Sar1p mutants did not affect the initiation or expansion of the sequestering membranes nor the trafficking of Atg11p and Atg9p to these membranes during micropexophagy. However, the lipidation of Atg8p and assembly of the micropexophagic membrane apparatus, which are essential to complete the incorporation of the peroxisomes into the degradative vacuole, were inhibited when either Sar1p mutant protein was expressed. During macropexophagy, the expression of sar1pT34N inhibited the formation of the pexophagosome, whereas sar1pH79G suppressed the delivery of the peroxisome from the pexophagosome to the vacuole. The pexophagosome contained Atg8p in wild-type cells, but in cells expressing sar1pH79G these organelles contain both Atg8p and endoplasmic reticulum components as visualized by DsRFP-HDEL. Our results demonstrate key roles for Sar1p in both micro- and macropexophagy.

scholarly journals Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. The role of guanosine triphosphate

1972 ◽  
Vol 126 (4) ◽  
pp. 933-943 ◽  
Author(s):  
J. Hradec
Keyword(s):  
Rat Liver ◽  
Ternary Complex ◽  
Cellulose Nitrate ◽  
Stable Complex ◽  
Bacterial Cells ◽  
Guanosine Triphosphate ◽  
Binding Reaction ◽  
Aminoacyl Transfer ◽  
Liver Ribosomes

1. Transferase I from rat liver binds relatively low quantities of GTP when incubated with this nucleotide in the absence of aminoacyl-tRNA. 2. Transferase I reacts with both aminoacyl-tRNA and GTP to form a relatively stable complex that is retained on cellulose nitrate filters. The ternary complex transferase I–aminoacyl-tRNA–GTP is also formed when the transferase I–aminoacyl-tRNA complex is incubated with GTP or during the incubation of the transferase I–GTP complex with aminoacyl-tRNA. Synthesis of this complex does not require the presence of Mg2+. 3. In the presence of Mg2+ the ternary complex becomes readily bound to ribosomes without requirements for any other cofactors. 4. An extensive cleavage of GTP takes place when aminoacyl-tRNA becomes bound to ribosomes. 5. The low interdependence of reactions leading to the formation of transferase I complexes with aminoacyl-tRNA and GTP indicates that the mechanisms of the binding reaction in mammalian systems may be different from those in bacterial cells.

Peptide chain elongation: A possible role of montmorillonite in prebiotic synthesis of protein precursors

1995 ◽  
Vol 25 (5) ◽  
pp. 431-441 ◽  
Author(s):  
Juraj Bujdák ◽  
Katarína Faybíková ◽  
Artur Eder ◽  
Yongyos Yongyai ◽  
Bernd M. Rode
Keyword(s):  
Prebiotic Synthesis ◽  
Peptide Chain ◽  
Chain Elongation
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