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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.
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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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Unlike carbon, water, and nitrogen, phosphorus is not present in the atmosphere as a gas. Instead, most phosphorus in the ecosystem exists as compounds, such as phosphate ions (PO43-), found in soil, water, sediment and rocks. Phosphorus is often a limiting nutrient (i.e., in short supply). Consequently, phosphorus is added to most agricultural fertilizers, which can cause environmental problems related to runoff in aquatic ecosystems.
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Nitrogen atoms, present in all proteins and DNA, are recycled between abiotic and biotic components of the ecosystem. However, the primary form of nitrogen on Earth is nitrogen gas, which cannot be used by most animals and plants. Thus, nitrogen gas must first be converted into a usable form by nitrogen-fixing bacteria before it can be cycled through other living organisms. The use of nitrogen-containing fertilizers and animal waste products in human agriculture has greatly influenced the...
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Updated: Feb 4, 2026

Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
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Cycling around Lysine Modifications.

Surinder Kumar1, David B Lombard2

  • 1Department of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.

Trends in Biochemical Sciences
|June 10, 2017
PubMed
Summary
This summary is machine-generated.

New protein modifications called acyl-lysine modifications impact cell functions. Research offers chemical insights into the mechanisms of protein acylation, a key cellular process.

Keywords:
HMGylationMGcylationMGylationSIRT4non-enzymatic acylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Recent research has uncovered numerous novel protein acyl-lysine modifications.
  • These modifications influence the function of proteins in various cellular processes.

Purpose of the Study:

  • To provide new chemical insights into the mechanisms of protein acylation.
  • To deepen the understanding of the role of protein acyl-lysine modifications in cellular functions.

Main Methods:

  • The study involved detailed chemical analysis of protein acylation.
  • Investigated the mechanisms underlying the formation and function of acyl-lysine modifications.

Main Results:

  • Identified a wide range of previously unknown protein acyl-lysine modifications.
  • Elucidated novel chemical mechanisms involved in protein acylation.
  • Demonstrated the significant impact of these modifications on cellular processes.

Conclusions:

  • Protein acylation, particularly acyl-lysine modifications, plays a crucial role in regulating cellular functions.
  • Further research into these modifications can reveal new therapeutic targets.