Stabilization by the 30S ribosomal subunit of the interaction of 50S subunits with elongation factor G and guanine nucleotide

Biochemistry ◽  
1977 ◽  
Vol 16 (7) ◽  
pp. 1278-1283 ◽  
Author(s):  
Robert C. Marsh ◽  
Andrea Parmeggiani
Keyword(s):  
Ribosomal Subunit ◽  
Elongation Factor ◽  
Guanine Nucleotide ◽  
Elongation Factor G ◽  
Factor G

scholarly journals Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation

2009 ◽  
Vol 106 (37) ◽  
pp. 15702-15707 ◽  
Author(s):  
Jingyi Fei ◽  
Jonathan E. Bronson ◽  
Jake M. Hofman ◽  
Rathi L. Srinivas ◽  
Chris H. Wiggins ◽  
...  
Keyword(s):  
Dynamic Equilibrium ◽  
Ribosomal Subunit ◽  
Elongation Factor ◽  
Large Ribosomal Subunit ◽  
Elongation Factor G ◽  
Structural Element ◽  
Time Dynamics ◽  
Kinetic Mechanisms ◽  
Trna Translocation ◽  
Factor G

Determining the mechanism by which tRNAs rapidly and precisely transit through the ribosomal A, P, and E sites during translation remains a major goal in the study of protein synthesis. Here, we report the real-time dynamics of the L1 stalk, a structural element of the large ribosomal subunit that is implicated in directing tRNA movements during translation. Within pretranslocation ribosomal complexes, the L1 stalk exists in a dynamic equilibrium between open and closed conformations. Binding of elongation factor G (EF-G) shifts this equilibrium toward the closed conformation through one of at least two distinct kinetic mechanisms, where the identity of the P-site tRNA dictates the kinetic route that is taken. Within posttranslocation complexes, L1 stalk dynamics are dependent on the presence and identity of the E-site tRNA. Collectively, our data demonstrate that EF-G and the L1 stalk allosterically collaborate to direct tRNA translocation from the P to the E sites, and suggest a model for the release of E-site tRNA.

scholarly journals Control of Ribosomal Subunit Rotation by Elongation Factor G

Science ◽  
2013 ◽  
Vol 340 (6140) ◽  
pp. 1235970 ◽  
Author(s):  
Arto Pulk ◽  
Jamie H. D. Cate
Keyword(s):  
Messenger Rna ◽  
Ribosomal Subunit ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Elongation Factor G ◽  
Before And After ◽  
Switch Regions ◽  
Subunit Rotation ◽  
Guanosine Triphosphatase ◽  
Factor G

Protein synthesis by the ribosome requires the translocation of transfer RNAs and messenger RNA by one codon after each peptide bond is formed, a reaction that requires ribosomal subunit rotation and is catalyzed by the guanosine triphosphatase (GTPase) elongation factor G (EF-G). We determined 3 angstrom resolution x-ray crystal structures of EF-G complexed with a nonhydrolyzable guanosine 5′-triphosphate (GTP) analog and bound to the Escherichia coli ribosome in different states of ribosomal subunit rotation. The structures reveal that EF-G binding to the ribosome stabilizes switch regions in the GTPase active site, resulting in a compact EF-G conformation that favors an intermediate state of ribosomal subunit rotation. These structures suggest that EF-G controls the translocation reaction by cycles of conformational rigidity and relaxation before and after GTP hydrolysis.

scholarly journals Conformational Changes of the Small Ribosomal Subunit During Elongation Factor G-dependent tRNA–mRNA Translocation

2004 ◽  
Vol 343 (5) ◽  
pp. 1183-1194 ◽  
Author(s):  
Frank Peske ◽  
Andreas Savelsbergh ◽  
Vladimir I. Katunin ◽  
Marina V. Rodnina ◽  
Wolfgang Wintermeyer
Keyword(s):  
Conformational Changes ◽  
Ribosomal Subunit ◽  
Elongation Factor ◽  
Elongation Factor G ◽  
Small Ribosomal Subunit ◽  
Factor G

scholarly journals Coordinate Inhibition of Elongation Factor G Function and Ribosomal Subunit Association by Antibodies to Several Ribosomal Proteins

1974 ◽  
Vol 71 (3) ◽  
pp. 627-630 ◽  
Author(s):  
J. H. Highland ◽  
E. Ochsner ◽  
J. Gordon ◽  
J. W. Bodley ◽  
R. Hasenbank ◽  
...  
Keyword(s):  
Ribosomal Proteins ◽  
Ribosomal Subunit ◽  
Elongation Factor ◽  
Elongation Factor G ◽  
Factor G

Contacts of Elongation Factor G with the Small Ribosomal Subunit: Cross-Linking Approach

2003 ◽  
Vol 393 (1-6) ◽  
pp. 312-315 ◽  
Author(s):  
A. V. Kubarenko ◽  
I. N. Lavrik ◽  
P. V. Sergiev ◽  
M. Heupl ◽  
M. Rodnina ◽  
...  
Keyword(s):  
Ribosomal Subunit ◽  
Elongation Factor ◽  
Cross Linking ◽  
Elongation Factor G ◽  
Small Ribosomal Subunit ◽  
Factor G
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