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Related Concept Videos

The Central Dogma01:20

The Central Dogma

The central dogma explains the flow of genetic information from DNA nucleotides to the amino acid sequence of proteins.
RNA is the Missing Link Between DNA and Proteins
In the early 1900s, scientists discovered that DNA stores all the information needed for cellular functions and that proteins perform most of these functions. However, the mechanisms of converting genetic information into functional proteins remained unknown for many years. Initially, it was believed that a single gene is...
The Central Dogma01:25

The Central Dogma

Overview
Nonsense-mediated mRNA Decay02:27

Nonsense-mediated mRNA Decay

The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
Usually, Upf3 binds to an Exon Junction Complex (EJC) at mRNA splice sites. If a ribosome fully translates the mRNA,...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
From DNA to Protein03:06

From DNA to Protein

The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
Leaky Scanning02:28

Leaky Scanning

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 stands for...

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Related Experiment Video

Updated: Jun 2, 2026

Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells
10:06

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Published on: April 26, 2017

A universal code for RNA recognition by PUF proteins.

Aleksandra Filipovska1, Muhammad F M Razif, Karoline K A Nygård

  • 1Western Australian Institute for Medical Research and Centre for Medical Research, The University of Western Australia, Perth, Australia.

Nature Chemical Biology
|May 17, 2011
PubMed
Summary
This summary is machine-generated.

Researchers engineered Pumilio and FBF homology protein (PUF) repeats to recognize and bind cytosine in RNA. This breakthrough enables the creation of PUF domains for targeted RNA binding, advancing biological and medical applications.

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Area of Science:

  • Molecular Biology
  • Protein Engineering
  • RNA Therapeutics

Background:

  • Designing proteins for specific RNA sequence recognition is crucial for biological and medical applications.
  • Existing Pumilio and FBF homology protein (PUF) repeats primarily recognize adenine, guanine, and uracil bases in RNA.

Purpose of the Study:

  • To expand the RNA recognition capabilities of PUF repeats beyond the standard bases.
  • To evolve PUF repeats for specific binding to cytosine.
  • To develop novel PUF domains for selective RNA targeting.

Main Methods:

  • Protein engineering of PUF repeats.
  • Directed evolution techniques to alter RNA sequence specificity.
  • Assays to confirm binding affinity and specificity for cytosine-containing RNA targets.

Main Results:

  • Successfully engineered PUF repeats that recognize and bind cytosine.
  • Demonstrated expanded RNA sequence recognition beyond adenine, guanine, and uracil.
  • Created novel PUF domains with selective binding capabilities for diverse RNA targets.

Conclusions:

  • The engineered PUF repeats represent a significant advancement in programmable RNA-binding proteins.
  • These novel PUF domains hold potential for diverse applications in molecular biology and medicine.
  • The ability to target specific RNA sequences, including those with cytosine, opens new avenues for therapeutic development.