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The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
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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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Related Experiment Video

Updated: Jan 5, 2026

Antibody-Free Assay for RNA Methyltransferase Activity Analysis
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Structural insight into human N6amt1-Trm112 complex functioning as a protein methyltransferase.

Wenjing Li1, Yu Shi1,2, Tianlong Zhang1

  • 11State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai, 200031 China.

Cell Discovery
|October 23, 2019
PubMed
Summary

Human N6amt1 is not a DNA methyltransferase. Structural and biochemical data show it is a protein methyltransferase, specifically methylating Gln185 of eRF1, not DNA.

Keywords:
Post-translational modificationsX-ray crystallography

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Structural Biology

Background:

  • DNA methylation, including N6-methyladenine (6mA), is crucial in bacteria and found in eukaryotes.
  • Human N6amt1 was controversially proposed as a 6mA DNA methyltransferase.

Purpose of the Study:

  • To determine the enzymatic activity and structural role of human N6amt1-Trm112 complex.
  • To resolve the controversy regarding N6amt1's function as a DNA methyltransferase.

Main Methods:

  • X-ray crystallography to determine the structure of N6amt1-Trm112 complex with SAM.
  • Biochemical assays to test DNA binding and methyltransferase activity.

Main Results:

  • The crystal structure revealed Trm112 stabilizes N6amt1 but is not involved in substrate binding.
  • N6amt1's active site is negatively charged, unsuitable for DNA binding.
  • Biochemical data confirmed N6amt1 lacks DNA methyltransferase activity but methylates Gln185 of eRF1.

Conclusions:

  • Human N6amt1 is a protein methyltransferase, not a DNA methyltransferase.
  • The study clarifies N6amt1's role in protein methylation, specifically eRF1 modification.