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Related Experiment Video

Updated: Jul 13, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

RNase A - tRNA binding alters protein conformation.

C N N'soukpoé-Kossi¹, C Ragi, H A Tajmir-Riahi

¹Department of Chemistry-Biology, Université du Québec at Trois-Rivières, C.P. 500 Trois-Rivières, QC G9A 5H7, Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire

|July 7, 2007

Summary

Bovine pancreatic ribonuclease A (RNase A) binds to transfer RNA (tRNA) at specific sites, forming complexes without digesting the RNA. This interaction alters the secondary structures of both RNase A and tRNA.

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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Bovine pancreatic ribonuclease A (RNase A) is known to cleave RNA at pyrimidine bases.
While RNase A interactions with nucleotides and oligonucleotides are well-studied, its complexation with transfer RNA (tRNA) remains less investigated.

Purpose of the Study:

To investigate the complexation of RNase A with tRNA in aqueous solution under physiological conditions.
To determine the binding mode, binding constant, sequence preference, and structural changes in the RNase A-tRNA complex.

Main Methods:

Spectroscopic techniques including Fourier transform infrared (FTIR), UV-visible, and circular dichroism (CD) spectroscopy were employed.
Constant RNA concentration with varying RNase A concentrations were used to study complex formation.

Main Results:

Two major binding sites for RNase A on tRNA were identified: G-C base pairs and the backbone PO2 group.
An overall binding constant (K) of 4.0 x 10^5 (mol/L)^-1 was determined for the RNase A-tRNA complex.
Protein-RNA interaction induced significant changes in RNase A secondary structure (reduced alpha helix and beta sheets, increased turn and random coil), while tRNA maintained its A-form conformation. No RNA digestion occurred.

Conclusions:

RNase A forms stable complexes with tRNA at specific sites without enzymatic degradation.
The interaction leads to substantial conformational changes in RNase A's secondary structure, indicating a regulatory role or altered function upon binding.