Chaperone (protein) in the context of "Chromosomes"

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⭐ Core Definition: Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis.

The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress.

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Chaperone (protein) in the context of Chromosome

A chromosome is a package of DNA containing part or all of the genetic material of an organism. In most chromosomes, the very long thin DNA fibers are coated with nucleosome-forming packaging proteins; in eukaryotic cells, the most important of these proteins are the histones. Aided by chaperone proteins, the histones bind to and condense the DNA molecule to maintain its integrity. These eukaryotic chromosomes display a complex three-dimensional structure that has a significant role in transcriptional regulation.

Normally, chromosomes are visible under a light microscope only during the metaphase of cell division, where all chromosomes are aligned in the center of the cell in their condensed form. Before this stage occurs, each chromosome is duplicated (S phase), and the two copies are joined by a centromere—resulting in either an X-shaped structure if the centromere is located equatorially, or a two-armed structure if the centromere is located distally; the joined copies are called 'sister chromatids'. During metaphase, the duplicated structure (called a 'metaphase chromosome') is highly condensed and thus easiest to distinguish and study. In animal cells, chromosomes reach their highest compaction level in anaphase during chromosome segregation.

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Chaperone (protein) in the context of Anaphase

Anaphase (from Ancient Greek ἀνα- (ana-) 'back, backward' and φάσις (phásis) 'appearance') is the stage of mitosis after the process of metaphase, when replicated chromosomes are split and the newly-copied chromosomes (daughter chromatids) are moved to opposite poles of the cell. Chromosomes also reach their overall maximum condensation in late anaphase, to help chromosome segregation and the re-formation of the nucleus.

Anaphase starts when the anaphase promoting complex marks an inhibitory chaperone called securin for destruction by ubiquitylating it. Securin is a protein which inhibits a protease known as separase. The destruction of securin unleashes separase which then breaks down cohesin, a protein responsible for holding sister chromatids together.

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