Histone octamer: Difference between revisions

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[[File:Basic units of chromatin structure.svg|thumb]] [[File:Histone Octamer x-ray structure.jpg|thumb]] [[File:Nucleosome structure.png|thumb]] Histone Octamer


The '''histone octamer''' is a core component of the nucleosome, which is the fundamental unit of chromatin structure in eukaryotic cells. The nucleosome plays a critical role in the organization and regulation of DNA, facilitating the compaction of DNA into the nucleus and influencing gene expression.
{{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 =
}}
 
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==
==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.


The histone octamer is composed of eight histone proteins: two each of [[Histone H2A|H2A]], [[Histone H2B|H2B]], [[Histone H3|H3]], and [[Histone H4|H4]]. These histones are highly conserved proteins that form a protein core around which approximately 147 base pairs of DNA are wrapped in 1.65 left-handed superhelical turns.
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.
 
===Histone Fold Domain===
 
Each histone protein contains a characteristic structural motif known as the "histone fold," which consists of three alpha helices connected by two loops. This motif facilitates the dimerization of histones, allowing them to form H2A-H2B and H3-H4 dimers. Two H3-H4 dimers associate to form a tetramer, and two H2A-H2B dimers join this tetramer to complete the octamer.
 
===Assembly===
 
The assembly of the histone octamer is a highly regulated process that occurs in the cell nucleus. Initially, the H3-H4 tetramer binds to DNA, followed by the addition of two H2A-H2B dimers to form the complete nucleosome core particle. This assembly is facilitated by histone chaperones, which prevent non-specific interactions and ensure proper nucleosome formation.


==Function==
==Function==
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.


The primary function of the histone octamer is to package DNA into a compact, organized structure, allowing it to fit within the confines of the cell nucleus. This packaging also plays a crucial role in regulating access to the DNA, thereby influencing processes such as [[DNA replication]], [[DNA repair]], and [[transcription]].
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.


===Chromatin Remodeling===
==Role in Chromatin Dynamics==
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.


The positioning and composition of histone octamers can be altered by chromatin remodeling complexes, which use energy derived from ATP hydrolysis to reposition, eject, or restructure nucleosomes. This dynamic remodeling is essential for allowing access to DNA during transcription and other DNA-dependent processes.
==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.
===Histone Modifications===
 
Histone proteins within the octamer can undergo various post-translational modifications, such as acetylation, methylation, phosphorylation, and ubiquitination. These modifications occur primarily on the histone tails, which protrude from the nucleosome core, and play a key role in regulating chromatin structure and function. For example, acetylation of lysine residues is generally associated with transcriptional activation, while methylation can be associated with either activation or repression, depending on the specific residues modified.
 
==Also see==


==See also==
* [[Chromatin]]
* [[Nucleosome]]
* [[Nucleosome]]
* [[Chromatin]]
* [[Histone]]
* [[Histone modification]]
* [[Epigenetics]]
* [[Epigenetics]]
* [[Chromatin remodeling]]


{{Histones}}
==References==
<references />
 
{{Protein-stub}}


[[Category:Histones]]
[[Category:Chromatin]]
[[Category:Chromatin]]
[[Category:Histone proteins]]
[[Category:Epigenetics]]
[[Category:Molecular biology]]

Revision as of 04:35, 29 December 2024


Core component of chromatin 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

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

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

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

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

References

<references />


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