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Related Concept Videos

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...
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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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Related Experiment Video

Updated: Jun 15, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Genetically encoding ε-N-methacryllysine into proteins in live cells.

Tian-Yi Zhu1,2, Shi-Yi Chen1,2, Mengdi Zhang1,2

  • 1Department of Medical Oncology, The Second Affiliated Hospital of Zhejiang University School of Medicine, Life Science Institute, Zhejiang University, Hangzhou, Zhejiang, China.

Nature Communications
|March 18, 2025
PubMed
Summary
This summary is machine-generated.

Researchers identified lysine methacrylation (Kmea) on the non-histone protein Cyclophilin A (CypA). This post-translational modification regulates cellular redox homeostasis and can be further modified in live cells.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Post-Translational Modifications
  • Proteomics

Background:

  • Lysine acylation is a crucial post-translational modification (PTM) involved in diverse cellular functions.
  • While thousands of lysine acylation sites are known, only 27 lysine methacrylation (Kmea) sites have been identified, exclusively in histones.
  • Distinguishing Kmea from its isomer, lysine crotonylation (Kcr), poses biochemical challenges.

Purpose of the Study:

  • To identify Kmea sites on a non-histone protein, Cyclophilin A (CypA).
  • To investigate the functional roles of Kmea in CypA.
  • To develop a method for studying Kmea modification and its interactions in live cells.

Main Methods:

  • Identification of Kmea sites on Cyclophilin A (CypA).
  • Genetic code expansion to incorporate ε-N-Methacryllysine (MeaK), a non-canonical amino acid (ncAA), into target proteins.
  • Affinity-purification mass spectrometry (MS) to identify proteins interacting with methacrylated CypA.

Main Results:

  • Kmea was identified on the non-histone protein CypA.
  • Kmea at CypA site 125 was found to regulate cellular redox homeostasis.
  • HDAC1 was identified as a regulator of Kmea on CypA, and genetically encoded Kmea can be further methylated to ε-N-methyl-ε-N-methacrylation (Kmemea) in live cells.

Conclusions:

  • This study expands the known landscape of Kmea modifications beyond histones to non-histone proteins like CypA.
  • Kmea on CypA plays a significant role in regulating cellular redox balance.
  • The developed genetic code expansion approach provides a powerful tool for studying Kmea functions and interactions in vivo.