Evidence for the structural stability of ribonucleoprotein LMG(160) under ribonuclease-A treatment
Maryam Shahhoseini1, Azra Rabbani Chadegani, Sayeh Abdosamadi
1Department of Biochemistry, Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Abstract:
Low mobility group nonhistone protein, LMG(160), is a ribonucleoprotein particle of the nuclear matrix with an inhibitory effect on transcription. Through the current study, we have investigated comparatively the effect and behavior of the protein in the absence and presence of its RNA moiety. Analysis was performed with the intact LMG(160) and its RNase-treated form using native and denatured gel electrophoresis as well as fluorescence spectroscopy and trypsin digestion techniques. The results show that the RNA moiety of LMG(160) plays a key role in maintaining the overall structure and conformation of this RNP particle, in the way that RNA removal causes some alterations in the structural stability of the protein, leading it to become self-associated. This finding can easily explain the loss of function of LMG(160) after RNase-treatment, the effect that may influence the biological activity of the molecule in the nuclear matrix structure.
Related Concept Videos
RNA Stability
RNA Stability
Ribozymes
Ribozymes can be...
Ribozymes
Ribozymes can be...
Ribosome Profiling
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique helps...
Ribosomal RNA Synthesis
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...

