Protein-free ribosomal RNA scaffolds can assemble poly-lysine oligos from charged tRNA fragments.

Biochem Biophys Res Commun

Department of Biology and Biochemistry, University of Houston, Houston, TX, 77204, USA. Electronic address:

Published: March 2021

Ribosomal protein synthesis is a central process of the modern biological world. Because the ribosome contains proteins itself, it is very important to understand its precursor and evolution. Small ribozymes have demonstrated the principle of "RNA world" hypothesis, but protein free peptide ligase remains elusive. In this report, we have identified two fragments in the peptidyl transfer center that can synthesize a 9-mer poly-lysine in a solution contains Mg. This result is deduced from isotope-shifting in high resolution MS. To our best knowledge, this is the longest peptide oligo that can be synthesized by a pure ribozyme. Via single molecule FRET experiments, we have demonstrated the ligase mechanism was probably by substrate proximity via dimerization. We prospect that these RNA fragments can be useful to synthesize template free natural and non-natural peptides, to be model system for peptidyl transfer reaction mechanism and can shed light to the evolution of ribosome.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936610PMC
http://dx.doi.org/10.1016/j.bbrc.2021.01.036DOI Listing

Publication Analysis

Top Keywords

peptidyl transfer
8
protein-free ribosomal
4
ribosomal rna
4
rna scaffolds
4
scaffolds assemble
4
assemble poly-lysine
4
poly-lysine oligos
4
oligos charged
4
charged trna
4
trna fragments
4

Similar Publications

Structural insights into context-dependent inhibitory mechanisms of chloramphenicol in cells.

Nat Struct Mol Biol

December 2024

Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.

Ribosome-targeting antibiotics represent an important class of antimicrobial drugs. Chloramphenicol (Cm) is a well-studied ribosomal peptidyl transferase center (PTC) binder and growing evidence suggests that its inhibitory action depends on the sequence of the nascent peptide. How such selective inhibition on the molecular scale manifests on the cellular level remains unclear.

View Article and Find Full Text PDF

A primary precursor of jasmonates 12-oxo-phytodienoic acid (OPDA) is an autonomous hormone signal that activates and fine-tunes plant defense responses, as well as growth and development. However, the architecture of its signaling circuits remains largely elusive. Here we describe that OPDA signaling drives photosynthetic reductant powers toward the plastid sulfur assimilations, incorporating sulfide into cysteine.

View Article and Find Full Text PDF

Rhomboid proteases are ubiquitous intramembrane serine proteases that can cleave transmembrane substrates within lipid bilayers. They exhibit many and diverse functions, such as but not limited to, growth factor signaling, immune and inflammatory response, protein quality control, and parasitic invasion. Human rhomboid protease RHBDL4 has been demonstrated to play a critical role in removing misfolded proteins from the Endoplasmic Reticulum and is implicated in severe diseases such as various cancers and Alzheimer's disease.

View Article and Find Full Text PDF

ACE2 alleviates sepsis-induced cardiomyopathy through inhibiting M1 macrophage via NF-κB/STAT1 signals.

Cell Biol Toxicol

September 2024

Department of Emergency Medicine, Beijing Key Laboratory of Cardiopulmonary Cerebral Resuscitation, Beijing Chao-Yang Hospital, Capital Medical University, No. 8 Worker's Stadium South Roud, Beijing, 100020, China.

Angiotensin-converting enzyme 2 (ACE2), a crucial element of the renin-angiotensin system (RAS), metabolizes angiotensin II into Ang (1-7), which then combines with the Mas receptor (MasR) to fulfill its protective role in various diseases. Nevertheless, the involvement of ACE2 in sepsis-induced cardiomyopathy (SIC) is still unexplored. In this study, our results revealed that CLP surgery dramatically impaired cardiac function accompanied with disruption of the balance between ACE2-Ang (1-7) and ACE-Ang II axis in septic heart tissues.

View Article and Find Full Text PDF

EF-P is a translation factor that facilitates the formation of peptide bonds between consecutive prolines. Using FRET between EF-P and ribosomal protein bL33, we studied dynamics and specificity of EF-P binding to the ribosome. Our findings reveal that EF-P rapidly scans for a free E site and can bind to any ribosome containing a P-site tRNA, regardless of the ribosome's functional state.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!