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Related Concept Videos

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
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RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Expression Analysis of Mammalian Linker-histone Subtypes
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Human m6A writers: Two subunits, 2 roles.

Xiang Wang1, Jinbo Huang1, Tingting Zou1,2

  • 1a National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Huazhong Agricultural University , Wuhan , China.

RNA Biology
|January 26, 2017
PubMed
Summary

The N6-methyladenosine (m6A) methyltransferase complex, crucial for RNA modification, has had its structure elucidated. This reveals METTL3 as catalytic and METTL14 as a stabilizer, advancing m6A research.

Keywords:
EpigeneticsMETTL3WTAPm6Amethyltransferase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Cellular RNAs undergo diverse chemical modifications, with N6-methyladenosine (m6A) being a prevalent internal modification on mRNA and non-coding RNAs.
  • m6A modification plays a critical role in various biological processes.

Purpose of the Study:

  • To detail the mechanism and subunit properties of the human m6A methyltransferase complex.
  • To understand the structural and biochemical characteristics of the METTL3-METTL14 complex.

Main Methods:

  • Recent structural determination of the m6A methyltransferase complex by three independent groups.
  • Biochemical characterization of individual subunits and the complex.

Main Results:

  • METTL3 functions as the primary catalytic subunit, similar to N6-adenine DNA methyltransferases.
  • METTL14 acts as a pseudomethyltransferase, stabilizing METTL3 and aiding RNA target recognition.
  • Structural and biochemical data elucidate the complex's mechanism.

Conclusions:

  • Understanding the m6A methyltransferase complex structure and function is key to deciphering m6A modification's biological roles.
  • This research provides a foundation for developing novel m6A-related therapeutic strategies.