3'-flap-structured DNA binding

Definition

Target type: molecularfunction

Binding to a 3'-flap structure in DNA. A DNA flap structure is one in which a single-stranded 3'-end of DNA or RNA protrudes from a double-stranded DNA molecule. [GOC:mah, PMID:15189154]

3'-flap-structured DNA binding is a molecular function that describes the interaction of proteins with a specific DNA structure known as a 3'-flap. This structure is characterized by a single-stranded DNA overhang, or "flap," that is extending from a double-stranded DNA molecule. 3'-flap-structured DNA binding proteins play crucial roles in various cellular processes, including DNA replication, repair, and recombination.

During DNA replication, 3'-flap structures can arise as intermediates in the process of Okazaki fragment maturation. These structures are generated when the lagging strand is synthesized in short fragments, called Okazaki fragments. The 3'-flap is removed by specialized enzymes, such as flap endonucleases, which bind to the 3'-flap structure and cleave the phosphodiester backbone, allowing for the ligation of the Okazaki fragments.

In DNA repair, 3'-flap structures can arise as a result of DNA damage. These structures can be generated by various mechanisms, such as nucleotide excision repair, where a damaged segment of DNA is excised and replaced with a new segment. The 3'-flap is then removed by specialized repair enzymes, such as flap endonucleases, to complete the repair process.

In DNA recombination, 3'-flap structures can be intermediates in the process of homologous recombination, where genetic information is exchanged between two DNA molecules. During homologous recombination, 3'-flap structures are generated by the strand invasion process, where a single-stranded DNA molecule invades a double-stranded DNA molecule. The 3'-flap is then processed by specialized enzymes, such as the Rad51 recombinase, to facilitate the exchange of genetic information between the two DNA molecules.

The 3'-flap-structured DNA binding function is typically associated with a specific protein domain or motif that recognizes and binds to the 3'-flap structure. These domains often contain specific amino acid residues that interact with the single-stranded DNA overhang, contributing to the stability and specificity of the protein-DNA interaction. By specifically recognizing and binding to 3'-flap structures, these proteins are able to regulate critical cellular processes, ensuring the accurate replication, repair, and recombination of DNA.'
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Proteins (1)

Compounds (2)