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Related Concept Videos

Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

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In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
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Translational Regulation01:29

Translational Regulation

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Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Related Experiment Video

Updated: Jan 17, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Understanding RNA Chaperone Activity of ProQ Protein.

Shilpi Singh1, Nisha Kumari1, Tanmay Dutta1

  • 1Department of Chemistry, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India.

Journal of Chemical Information and Modeling
|September 17, 2025
PubMed
Summary

Researchers explored the RNA chaperone ProQ

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • RNA-binding proteins (RBPs) regulate gene expression.
  • Hfq is a known bacterial RNA chaperone.
  • ProQ is a newly discovered RNA chaperone interacting with RaiZ sRNA.

Purpose of the Study:

  • To elucidate the molecular mechanism of RaiZ RNA binding to ProQ.
  • To investigate the role of specific residues in ProQ-RNA interactions.
  • To understand ProQ's RNA chaperone activity at an atomic level.

Main Methods:

  • Atomistic molecular dynamics simulations.
  • Enhanced sampling simulations (OPES_E).
  • In-silico mutagenesis studies.

Main Results:

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MS2-Affinity Purification Coupled with RNA Sequencing in Gram-Positive Bacteria
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Last Updated: Jan 17, 2026

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  • RaiZ RNA binds to ProQ's concave surface, stabilized by electrostatic interactions with polar and positively charged residues (arginine, lysine).
  • In-silico mutations of these key residues disrupt RNA binding.
  • Free energy surface analysis identified stable bound states and intermediate states of ProQ-RaiZ complex.

Conclusions:

  • ProQ utilizes electrostatic interactions for RaiZ RNA binding.
  • The study provides atomic-level insights into ProQ's RNA chaperone mechanism.
  • Findings enhance understanding of ProQ function in gene regulation.