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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Ribosomal RNA Synthesis02:53

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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,...
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Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Related Experiment Video

Updated: May 15, 2025

The MultiBac Protein Complex Production Platform at the EMBL
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The MultiBac Protein Complex Production Platform at the EMBL

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Argonaute-driven programmable multi-enzyme complex assembly on ribosomal RNA scaffolds.

Guangbo Yan1, Xia Li1, Xiaolan Yu1

  • 1State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.

International Journal of Biological Macromolecules
|May 7, 2025
PubMed
Summary

Researchers developed a novel RNA scaffold system using Argonaute (Ago) to organize enzymes for enhanced biocatalysis. This programmable system boosts in vitro cascade reaction efficiency, offering a versatile platform for multi-enzyme assembly.

Keywords:
ATP synthesisArgonauteFRETMulti-enzyme complexRNA scaffold

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Area of Science:

  • Biocatalysis
  • Molecular Biology
  • Synthetic Biology

Background:

  • Scaffold-based strategies enhance biocatalysis via enzyme spatial organization.
  • DNA and protein scaffolds are common, but RNA scaffolds offer unique advantages like flexibility and dynamic regulation.
  • In vitro applications of RNA scaffolds are limited by stability and cost concerns.

Purpose of the Study:

  • To develop a programmable RNA scaffold system for in vitro multi-enzyme assembly.
  • To enhance catalytic efficiency of multi-enzyme complexes using Argonaute-mediated assembly.
  • To demonstrate the adaptability and dynamic reconfiguration of enzyme arrangements.

Main Methods:

  • Utilized catalytically inactive MbpAgo to spatially organize enzymes on RNA scaffolds.
  • Employed guide DNAs (gDNAs) for directed assembly of MbpAgo-enzyme complexes onto yeast ribosomal RNA.
  • Used Förster resonance energy transfer (FRET) to confirm tunable protein localization.

Main Results:

  • Achieved precise positioning of three enzymes in the ATP biosynthesis pathway.
  • Demonstrated a 5.5-fold increase in catalytic yield after 3 hours compared to scaffold-free systems.
  • Showcased dynamic reconfiguration of enzyme arrangements by modifying gDNAs.

Conclusions:

  • Argonaute-mediated RNA scaffolds provide a versatile and efficient platform for in vitro multi-enzyme assembly.
  • The developed system significantly enhances catalytic efficiency in cascade reactions.
  • Programmable RNA scaffolds offer a promising approach for advancing biocatalysis.