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The aggregation, arrangement and bonding together of a nucleosome, the beadlike structural units of eukaryotic chromatin composed of histones and DNA. The aggregation, arrangement and bonding together of proteins on DNA to form the complex that mediates dosage compensation on the X chromosome of the heterogametic sex, ultimately resulting in a two-fold increase in transcription from this chromosome. An example of this is found in Drosophila melanogaster. The aggregation, arrangement and bonding together of proteins on promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription. The aggregation, arrangement and bonding together of a set of macromolecules to form a complex. The aggregation, arrangement and bonding together of proteins and DNA molecules to form a protein-DNA complex. The aggregation, arrangement and bonding together of proteins on DNA to form the complex that mediates dosage compensation on both X chromosomes in the monogametic sex, ultimately resulting in a two-fold reduction in transcription from these chromosomes. An example of this process is found in Caenorhabditis elegans. The aggregation, arrangement and bonding together of a set of components to form a telosome. A telosome is a nuclear telomere cap complex that is formed by the association of telomeric ssDNA- and dsDNA-binding proteins with telomeric DNA, and is involved in telomere protection and recruitment of telomerase. The aggregation, arrangement and bonding together of proteins and centromeric DNA molecules to form a centromeric protein-DNA complex. Includes the formation of the chromatin structures which form a platform for the kinetochore, and assembly of the kinetochore onto this specialized chromatin. In fission yeast and higher eukaryotes this process also includes the formation of heterochromatin at the outer repeat (pericentric) regions of the centromere. The aggregation, arrangement and bonding together of proteins and DNA molecules to form a protein-DNA complex, in which the complex is formed through interaction of the protein(s) with a interferon-stimulated response element (ISRE) in the DNA. The aggregation, arrangement and bonding together of strand exchange proteins (recombinases) into higher order oligomers on single-stranded DNA. The aggregation, arrangement and bonding together of proteins on DNA to form the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage. This assembly occurs before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage. The aggregation, arrangement and bonding together of a set of components to form the DNA replication preinitiation complex, a protein-DNA complex that is assembled at eukaryotic DNA replication origins immediately prior to the initiation of DNA replication, by the assembly of additional proteins onto an existing prereplicative complex. Any process carried out at the cellular level by which macromolecules aggregate, disaggregate, or are modified, resulting in the formation, disassembly, or alteration of a macromolecular complex. The aggregation, arrangement and bonding together of a set of components to form the pre-replicative complex, a protein-DNA complex that forms at eukaryotic DNA replication origins during late M phase; its presence is required for replication initiation. The aggregation, arrangement and bonding together of a set of macromolecules to form a complex, carried out at the cellular level.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein-DNA complex assembly
Acc: GO:0065004
Aspect: Biological Process
Desc: The aggregation, arrangement and bonding together of proteins and DNA molecules to form a protein-DNA complex.
Synonyms:
  • DNA-protein complex assembly
Proteins in PDR annotated with:
   This term: 11 [Search]
   Term or descendants: 475 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0065004 - protein-DNA complex assembly (interactive image map)
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Created and Maintained by: Michael Riffle