Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Ribozymes02:47

Ribozymes

13.3K
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...
13.3K
Leaky Scanning02:28

Leaky Scanning

5.6K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.6K
Ribosome Profiling02:24

Ribosome Profiling

4.0K
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...
4.0K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

32.4K
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
32.4K
RNA Stability01:53

RNA Stability

35.6K
Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
35.6K
Nucleic Acids02:43

Nucleic Acids

49.5K
Nucleic acids are the most important macromolecules for the continuity of life. They carry the cell's genetic blueprint and carry instructions for its functioning.
DNA and RNA
The two main types of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). DNA is the genetic material in all living organisms, ranging from single-celled bacteria to multicellular mammals. It is in the nucleus of eukaryotes and in the organelles, chloroplasts, and mitochondria. In prokaryotes,...
49.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Ubiquitination Defect of XIAP as Novel Susceptibility to Invasive Fungal Pneumonia.

The Journal of infectious diseases·2026
Same author

Self-Assembly of Stimuli-Responsive Peptide Enhances Therapeutics by Specifically Disrupting Hepatocellular Carcinoma Lysosomes In Vivo.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

Unified genomic and chemical representations enable bidirectional biosynthetic gene cluster and natural product retrieval.

Scientific reports·2026
Same author

Accelerating natural product discovery with linked MS-genomics and language/transformer-based models.

npj antimicrobials and resistance·2026
Same author

Ancestral sequence reconstruction reveals new functional fluorinases and mechanistic insights into enzymatic fluorination.

Chemical communications (Cambridge, England)·2026
Same author

A Singapore-centric Fungal Dataset of 518 Cultivated Strains with Visual Phenotypes and Taxonomic Identity.

Scientific data·2026
Same journal

A Multitask Prediction Framework for CircRNAs, Drugs, and Diseases Based on Multi-View Information Integration and Graph Contrastive Learning.

ACS synthetic biology·2026
Same journal

Engineering Modular Cargo Loading Strategies for Carboxysome-Derived Protein Particles.

ACS synthetic biology·2026
Same journal

Suppression of Salmonella Effectors with CRISPRi Controls the Immune Response to Bacterial Therapies.

ACS synthetic biology·2026
Same journal

Rational Design of Linalool Dehydratase-Isomerase Enables Efficient Conversion of Phytol to Neophytadiene.

ACS synthetic biology·2026
Same journal

<i>De Novo</i> Biosynthesis of Polyphyllin V in <i>Nicotiana benthamiana</i> through Pathway Reconstruction and UDP-Sugar Engineering.

ACS synthetic biology·2026
Same journal

Rapid and Continuous Directed Evolution in <i>Vibrio natriegens</i> Utilizing an <i>In Vivo</i> Hypermutation System.

ACS synthetic biology·2026
See all related articles

Related Experiment Video

Updated: Jan 9, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

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

Published on: August 9, 2019

7.1K

Design of a Labile RNase A Using Protein Language Models.

Gabriel Ong1, Kiat Whye Kong2, Si En Poh2

  • 1Institute of Sustainability for Chemicals, Energy and Environment, A*STAR, Singapore, 627833, Singapore.

ACS Synthetic Biology
|December 5, 2025
PubMed
Summary
This summary is machine-generated.

Researchers engineered a less stable enzyme variant, TempRNase, that retains RNA degradation activity but is easily inactivated. This offers a streamlined alternative for molecular biology workflows by simplifying enzyme removal and reducing experimental complexity.

Keywords:
Protein designprotein engineeringprotein language modelsribonuclease

More Related Videos

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA
13:00

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA

Published on: December 2, 2009

12.2K
An Oligonucleotide-based Tandem RNA Isolation Procedure to Recover Eukaryotic mRNA-Protein Complexes
09:45

An Oligonucleotide-based Tandem RNA Isolation Procedure to Recover Eukaryotic mRNA-Protein Complexes

Published on: August 18, 2018

11.5K

Related Experiment Videos

Last Updated: Jan 9, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

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

Published on: August 9, 2019

7.1K
A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA
13:00

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA

Published on: December 2, 2009

12.2K
An Oligonucleotide-based Tandem RNA Isolation Procedure to Recover Eukaryotic mRNA-Protein Complexes
09:45

An Oligonucleotide-based Tandem RNA Isolation Procedure to Recover Eukaryotic mRNA-Protein Complexes

Published on: August 18, 2018

11.5K

Area of Science:

  • Biochemistry
  • Protein Engineering
  • Molecular Biology

Background:

  • Protein language models (PLMs) are advanced tools for generating functional protein sequences.
  • Current research prioritizes enhancing protein stability for industrial uses, overlooking the potential of designing less stable proteins.
  • Easily inactivated enzymes can simplify molecular biology workflows by eliminating the need for physical removal after use.

Purpose of the Study:

  • To explore the engineering of functional, yet less stable proteins using Ribonuclease A (RNase A) as a model.
  • To develop a protein variant with reduced stability that retains enzymatic activity but is easily inactivated.
  • To demonstrate the concept of engineering "worst of the best" enzymes.

Main Methods:

  • Utilized protein language models (PLMs) to sample sequences from the embedding space near wild-type RNase A.
  • Engineered a variant, TempRNase, designed for reduced stability while maintaining RNA degradation function.
  • Employed a fluorometric RNA degradation assay to assess TempRNase stability under heat and reducing conditions.

Main Results:

  • Successfully engineered TempRNase, a variant of RNase A with significantly reduced stability.
  • Demonstrated that moderate heat and reducing treatments permanently inactivate TempRNase, with minimal impact on wild-type RNase A.
  • Sequence and structural analyses provided insights into the mechanisms of stability modulation and protein dynamics.

Conclusions:

  • Established the feasibility of engineering functional but less stable proteins, termed "worst of the best" enzymes.
  • RNase A serves as an effective model system for quantitatively tuning protein stability.
  • The developed TempRNase offers a promising tool for simplifying molecular biology protocols through controlled inactivation.