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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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Spreading of Chromatin Modifications02:25

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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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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Inheritance of Chromatin Structures03:17

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Analysis of Histone Antibody Specificity with Peptide Microarrays
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SETD3 functions beyond histidine methylation.

Rui Gao1, Hao Yang1, Yan Wang1

  • 1Institute of Cardiovascular Diseases, Xiamen Cardiovascular Hospital, School of medicine, Xiamen University, Xiamen 361000, China.

Life Sciences
|September 19, 2024
PubMed
Summary
This summary is machine-generated.

SETD3, a protein methyltransferase, regulates cell differentiation, tumorigenesis, and viral infection. This review explores its functions beyond histidine methylation, detailing its actions and regulation.

Keywords:
CancerDevelopmentDiseaseMethyltransferaseSETD3

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • SETD3 is identified as the first metazoan protein (actin) histidine methyltransferase.
  • SETD3 participates in crucial biological processes including cell differentiation, tumorigenesis, and viral infection.

Purpose of the Study:

  • To review the diverse biological roles of SETD3 beyond its established methyltransferase activity.
  • To elucidate the cellular and molecular mechanisms underlying SETD3's functions.
  • To summarize the upstream regulatory pathways affecting SETD3.

Main Methods:

  • Literature review and synthesis of existing research on SETD3.
  • Analysis of studies detailing SETD3's molecular functions and biological involvement.
  • Compilation of data on SETD3's regulation and modes of action.

Main Results:

  • SETD3 exhibits significant roles in cell differentiation, cancer development, and response to viral infections.
  • The protein's functions extend beyond actin histidine methylation, involving complex cellular pathways.
  • Upstream regulatory mechanisms controlling SETD3 activity and localization have been identified.

Conclusions:

  • SETD3 is a multifunctional protein critical for various physiological and pathological processes.
  • Understanding SETD3's broader roles provides insights into its potential as a therapeutic target.
  • Further research into SETD3 regulation and mechanisms will illuminate its involvement in disease.