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Related Concept Videos

Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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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.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Phase II Reactions: Methylation Reactions01:17

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Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
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Related Experiment Video

Updated: Dec 8, 2025

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

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Structural insight into HEMK2-TRMT112-mediated glutamine methylation.

Jie Gao1, Bin Wang2, Huijuan Yu1

  • 1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, P. R. China.

The Biochemical Journal
|September 24, 2020
PubMed
Summary

This study reveals how the HEMK2-TRMT112 complex methylates glutamine on eukaryotic release factor 1 (eRF1). Structural insights show HEMK2 uses a specific pocket for substrate recognition, clarifying protein glutamine methylation mechanisms.

Keywords:
HEMK2SAM/SAHTRMT112glutamine methylationx-ray crystallography

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Post-translational modifications regulate protein function in cellular events.
  • The HEMK2-TRMT112 heterodimer is known to methylate histone lysine and eukaryotic release factor 1 (eRF1) glutamine.
  • The mechanism of eRF1 glutamine methylation by HEMK2-TRMT112 is not well understood.

Purpose of the Study:

  • To elucidate the structural basis of HEMK2-TRMT112 recognition and catalysis of eRF1 glutamine methylation.
  • To understand the mechanism underlying protein glutamine methylation.
  • To investigate the dual methylation activity of HEMK2.

Main Methods:

  • X-ray crystallography to determine structures of HEMK2-TRMT112 complexed with SAM, and with SAH and methylglutamine (Qme).
  • Mass spectrometry to complement structural analyses.
  • Biochemical assays to study enzyme activity.

Main Results:

  • Two distinct structures of the HEMK2-TRMT112 complex were determined: one with SAM and another in a post-catalytic state with SAH and Qme.
  • Structural analysis revealed a specific pocket within HEMK2 that accommodates the glutamine substrate.
  • Mass spectrometry data supported the structural findings and indicated the catalytic mechanism.

Conclusions:

  • The study provides structural insights into the mechanism of protein glutamine methylation by the HEMK2-TRMT112 complex.
  • HEMK2 utilizes a dedicated pocket for recognizing and methylating glutamine residues.
  • This work highlights the dual catalytic activity of HEMK2, methylating both lysine and glutamine residues.