Related Experiment Video
Updated: Nov 2, 2025
06:52
Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
Published on: November 1, 2019
8.5K
Argonaute proteins: structures and their endonuclease activity.
Shujuan Jin1, Jian Zhan2, Yaoqi Zhou3,4,5
1Peking University Shenzhen Graduate School, Shenzhen, 518055, China.
Molecular Biology Reports
|June 12, 2021
Summary
Argonaute proteins are essential for gene silencing and defense against foreign nucleic acids. Recent studies highlight their structural and biological functions, revealing potential in gene editing applications.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Argonaute proteins are conserved across organisms, crucial for small RNA biogenesis.
- They mediate gene silencing pathways, defending against invading nucleic acids.
- These proteins function as nucleic-acid-guided endonucleases.
Purpose of the Study:
- To summarize recent advancements in Argonaute protein research.
- To explore the structural and biological aspects of Argonaute proteins.
- To identify potential applications of Argonaute proteins in gene editing.
Main Methods:
- Literature review of structural and biological studies.
- Analysis of Argonaute protein mechanisms in gene silencing.
- Evaluation of current and potential gene editing applications.
Main Results:
- Argonaute proteins guide small RNAs to target complementary DNA or RNA.
- Cleavage of targets leads to translational silencing, often involving accessory proteins.
- Structural and functional insights are rapidly expanding.
Conclusions:
- Argonaute proteins are versatile effectors in gene regulation and defense.
- Understanding their mechanisms provides a foundation for novel biotechnological tools.
- Argonaute proteins show significant promise for future gene editing technologies.
More Related Videos
Related Concept Videos
02:26Conservation of Protein Domains Over Different Proteins
13.5K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.5K
00:55DNA Helicases
22.9K
DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
22.9K
01:58Mechanical Protein Functions
5.2K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.
5.2K
02:47Ribozymes
12.9K
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...
Ribozymes can...
12.9K
01:11Restriction Enzymes
33.5K
Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
33.5K
02:02DNA Topoisomerases
33.2K
Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
33.2K