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Related Concept Videos

Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribosome Profiling02:24

Ribosome Profiling

Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
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 Synthesis02:53

Ribosomal RNA Synthesis

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,...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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,...
RNA Editing02:23

RNA Editing

RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...

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Related Experiment Video

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Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
10:05

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

Ribonuclease S redux.

Rex W Watkins1, Ulrich Arnold, Ronald T Raines

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, USA.

Chemical Communications (Cambridge, England)
|November 17, 2010
PubMed
Summary
This summary is machine-generated.

The S-peptide and S-protein of bovine pancreatic ribonuclease can noncovalently reassemble to restore enzyme activity. Modern techniques overcome previous limitations, enabling new applications for this protein fragment complementation system.

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Molecular Biology

Background:

  • The bovine pancreatic ribonuclease (RNase A) system, involving S-peptide and S-protein, is a classic example of protein fragment complementation.
  • This system has been historically significant in understanding protein folding and interactions.
  • However, inherent limitations have restricted its broader application in biochemical studies.

Purpose of the Study:

  • To re-evaluate the utility of the S-peptide/S-protein system from bovine pancreatic ribonuclease.
  • To demonstrate how modern biochemical methods can overcome the limitations of this system.
  • To explore new applications enabled by these improved methods.

Main Methods:

  • Utilizing advanced protein purification and characterization techniques.
  • Applying modern biochemical assays to assess enzymatic activity.
  • Developing novel experimental designs to leverage the complemented system.

Main Results:

  • The noncovalent complex of S-peptide and S-protein was successfully reconstituted, restoring ribonucleolytic activity.
  • Demonstrated that contemporary methods effectively address the historical limitations of the system.
  • Showcased the potential for novel applications of this protein fragment complementation system.

Conclusions:

  • The S-peptide/S-protein system remains a viable model for protein fragment complementation.
  • Modern techniques significantly enhance the utility and expand the applications of this system.
  • This work revitalizes a foundational system in protein chemistry for contemporary research.