The Formation of a Potential Spring in the Ribosome

Hedrick, Emily G.; Tanner, Douglas R.; Baig, Ahmad; Hill, Walter E.

doi:10.1016/j.jmb.2011.12.003

Cited by 2 publications

(2 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, we reported that such motion of the N-terminal arm of protein S12 is likely responsible for transient modification changes in the more distant helix 11 loop of 16S rRNA. 51 Such movement of the N-terminal arm of S12 may well cause base A909 to make initial or increased contact with base A1413 and that N 1 of base A1413 may be pushed into contact with N 1 of G1487, causing the time-dependent protections observed.…”

Section: Discussionmentioning

confidence: 99%

Real-Time Evidence for EF-G-Induced Dynamics of Helix 44 in 16S rRNA

Tanner

Hedrick

Hill

2012

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

The penultimate stem–loop of 16S ribosomal RNA (rRNA), helix 44, plays a central role in ribosome function. Using time-resolved dimethyl sulfate (DMS) probing, we have analyzed time-dependent modifications that occur at specific bases in this helix near the decoding region, resulting from the binding of elongation factor G (EF-G) in various forms. When EF-G-GTP is bound to 70S ribosomes, bases A1492 and A1493 are immediately protected, while other bases in the region show either no change or enhanced modification. When apo-EF-G is bound to 70S ribosomes and GTP is added, substantial transient time-dependent enhancement occurs at bases A1492 and A1493, with somewhat less enhancement occurring at base A1483, all in the first 45 ms. When mRNA and deacylated tRNAs are bound to the 70S ribosome and EF-G-GTP is added, bases A1492 and A1493 again show substantial and continued enhancement, while bases A1408, A1413, and A1418 all show time-dependent protection. These results provide primary, real-time evidence that EF-G induces direct or indirect structural changes in this region as EF-G is bound and as GTP is hydrolyzed.

show abstract

Section: Discussionmentioning

confidence: 99%

Real-Time Evidence for EF-G-Induced Dynamics of Helix 44 in 16S rRNA

Tanner

Hedrick

Hill

2012

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

show abstract

“…For T4 bacteriophage it is the contraction of the tail sheath that triggers structural rearrangements of baseplate proteins resulting in drilling of a hole in the bacterial cell wall followed by injection of its DNA . The ribosome translocates along the mRNA chain carrying tRNA molecules from one site on the ribosome to another, by undergoing a series of conformational changes fueled by GTP binding and hydrolysis …”

Section: Common Mechanistic Motifs In Large Protein Assembliesmentioning

confidence: 99%

Protein nanomachines assembly modes: cell‐free expression and biochip perspectives

Daube

Bar‐Ziv

2013

WIREs Nanomed Nanobiotechnol

View full text Add to dashboard Cite

Large macromolecular assemblies are widespread in all cell types with diverse structural and functional roles. Whether localized to membranes, nuclei, or cytoplasm, multimeric protein-nucleic acid complexes may be viewed as sophisticated nanomachines, an inspiration to chemical design. The formation of large biological assemblies follows a complex and hierarchical self-assembly process via ordered molecular recognition events. Serving a paradigm for biological assembly, extensive past studies of T4 bacteriophage and bacterial ribosomes by many groups have been revealing distinct design strategies, yet these two very different multimeric complexes share common mechanistic motifs. An emerging biochip approach highlights two conceptual notions to promote the study of assembly pathways: cell-free expression provides coupling between synthesis and assembly; surface anchoring allows high-resolution imaging of structural intermediates and opens up opportunities for rewiring a network by defining unnatural scaffolds for synthetic design applications.

show abstract

The Formation of a Potential Spring in the Ribosome

Cited by 2 publications

References 42 publications

Real-Time Evidence for EF-G-Induced Dynamics of Helix 44 in 16S rRNA

Real-Time Evidence for EF-G-Induced Dynamics of Helix 44 in 16S rRNA

Protein nanomachines assembly modes: cell‐free expression and biochip perspectives

Contact Info

Product

Resources

About