Histone octamer: Difference between revisions

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[[file:Basic_units_of_chromatin_structure.svg|thumb|Basic units of chromatin structure]] [[file:Histone_Octamer_x-ray_structure.jpg|thumb|Histone Octamer x-ray structure|left]] [[file:Nucleosome_structure.png|thumb|Nucleosome structure]] == Histone Octamer ==
{{Short description|Core component of chromatin structure}}
{{Infobox protein
| name = Histone octamer
| image = <!-- Image of histone octamer -->
| caption = Structure of the histone octamer
| symbol =
| pdb =
}}
[[File:Basic_units_of_chromatin_structure.svg|Basic units of chromatin structure|thumb]]
[[File:Nucleosome_structure.png|Nucleosome structure|thumb]]
The '''histone octamer''' is a core component of the [[nucleosome]], which is the fundamental unit of [[chromatin]] in [[eukaryotic cells]]. It consists of eight [[histone]] proteins: two each of [[histone H2A]], [[histone H2B]], [[histone H3]], and [[histone H4]]. These proteins form a complex around which [[DNA]] is wrapped, facilitating the compaction of DNA into the cell nucleus.


The '''histone octamer''' is a protein complex that plays a crucial role in the packaging of [[DNA]] into [[chromatin]] in [[eukaryotic cells]]. It is composed of eight histone proteins: two each of [[histone H2A]], [[histone H2B]], [[histone H3]], and [[histone H4]]. These histones form a core around which DNA winds, facilitating the compaction of DNA into the highly organized structure of chromatin.
==Structure==
The histone octamer is an octameric protein complex that forms the core of the nucleosome. Each octamer is composed of two copies of each of the four core histone proteins: H2A, H2B, H3, and H4. These histones are highly conserved proteins that play a critical role in the organization of chromatin.


=== Structure ===
The structure of the histone octamer is stabilized by interactions between the histone proteins, which include hydrogen bonds, hydrophobic interactions, and salt bridges. The histone fold domain, a characteristic structural motif found in all core histones, facilitates the formation of the histone octamer.
The histone octamer is an octameric assembly of histone proteins. Each histone protein has a characteristic structure that includes a central histone fold domain, which is involved in the formation of the histone octamer. The histone fold domain consists of three alpha helices connected by two loops. The histone octamer is formed by the interaction of these histone fold domains, creating a stable core around which DNA can wrap.


=== Function ===
==Function==
The primary function of the histone octamer is to package DNA into nucleosomes, the fundamental units of chromatin. Each nucleosome consists of approximately 147 base pairs of DNA wrapped around a histone octamer. This packaging reduces the length of DNA by about one-third, making it more compact and manageable within the cell nucleus. The histone octamer also plays a role in regulating gene expression by controlling the accessibility of DNA to transcription factors and other regulatory proteins.
The primary function of the histone octamer is to package DNA into a more compact, dense shape, allowing it to fit within the confines of the cell nucleus. This packaging also plays a crucial role in regulating [[gene expression]], as the accessibility of DNA to transcription factors and other proteins is influenced by its association with histones.


=== Assembly ===
Histone modifications, such as [[acetylation]], [[methylation]], and [[phosphorylation]], can alter the interaction between DNA and the histone octamer, thereby influencing chromatin structure and gene expression. These modifications are part of the [[epigenetic]] regulation of gene activity.
The assembly of the histone octamer is a highly regulated process that occurs in the cell nucleus. Histone proteins are synthesized in the cytoplasm and then transported into the nucleus, where they undergo post-translational modifications. These modifications, such as [[acetylation]], [[methylation]], and [[phosphorylation]], can influence the assembly and stability of the histone octamer. The histone proteins then interact with each other to form the histone octamer, which subsequently associates with DNA to form nucleosomes.


=== Histone Variants ===
==Role in Chromatin Dynamics==
In addition to the canonical histones, there are several histone variants that can replace the standard histones in the octamer. These variants, such as [[H2A.Z]], [[H3.3]], and [[CENP-A]], can alter the properties of the nucleosome and influence chromatin structure and function. Histone variants are often involved in specific cellular processes, such as [[DNA repair]], [[transcriptional regulation]], and [[chromosome segregation]].
The histone octamer is central to the dynamic nature of chromatin. During processes such as [[DNA replication]], [[transcription]], and [[DNA repair]], the nucleosome structure must be temporarily disrupted to allow access to the DNA. The histone octamer can be disassembled and reassembled as needed, a process facilitated by histone chaperones and chromatin remodeling complexes.


=== Related Pages ===
==Clinical Significance==
Alterations in histone proteins or their modifications can lead to various diseases, including [[cancer]]. Mutations in histone genes or dysregulation of histone-modifying enzymes can result in aberrant chromatin structures and misregulation of gene expression, contributing to oncogenesis.
 
==See also==
* [[Chromatin]]
* [[Chromatin]]
* [[Nucleosome]]
* [[Nucleosome]]
* [[Histone]]
* [[Histone]]
* [[DNA]]
* [[Epigenetics]]
* [[Gene expression]]
 
* [[Post-translational modification]]
==References==
* [[Transcription factor]]
<references />


[[Category:Cell biology]]
{{Protein-stub}}
[[Category:Genetics]]
[[Category:Molecular biology]]


{{Cell-biology-stub}}
[[Category:Histones]]
[[Category:Chromatin]]
[[Category:Epigenetics]]

Latest revision as of 20:52, 27 February 2025

Core component of chromatin structure


Basic units of chromatin structure
Nucleosome structure

The histone octamer is a core component of the nucleosome, which is the fundamental unit of chromatin in eukaryotic cells. It consists of eight histone proteins: two each of histone H2A, histone H2B, histone H3, and histone H4. These proteins form a complex around which DNA is wrapped, facilitating the compaction of DNA into the cell nucleus.

Structure[edit]

The histone octamer is an octameric protein complex that forms the core of the nucleosome. Each octamer is composed of two copies of each of the four core histone proteins: H2A, H2B, H3, and H4. These histones are highly conserved proteins that play a critical role in the organization of chromatin.

The structure of the histone octamer is stabilized by interactions between the histone proteins, which include hydrogen bonds, hydrophobic interactions, and salt bridges. The histone fold domain, a characteristic structural motif found in all core histones, facilitates the formation of the histone octamer.

Function[edit]

The primary function of the histone octamer is to package DNA into a more compact, dense shape, allowing it to fit within the confines of the cell nucleus. This packaging also plays a crucial role in regulating gene expression, as the accessibility of DNA to transcription factors and other proteins is influenced by its association with histones.

Histone modifications, such as acetylation, methylation, and phosphorylation, can alter the interaction between DNA and the histone octamer, thereby influencing chromatin structure and gene expression. These modifications are part of the epigenetic regulation of gene activity.

Role in Chromatin Dynamics[edit]

The histone octamer is central to the dynamic nature of chromatin. During processes such as DNA replication, transcription, and DNA repair, the nucleosome structure must be temporarily disrupted to allow access to the DNA. The histone octamer can be disassembled and reassembled as needed, a process facilitated by histone chaperones and chromatin remodeling complexes.

Clinical Significance[edit]

Alterations in histone proteins or their modifications can lead to various diseases, including cancer. Mutations in histone genes or dysregulation of histone-modifying enzymes can result in aberrant chromatin structures and misregulation of gene expression, contributing to oncogenesis.

See also[edit]

References[edit]

<references />


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