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Search results 1 to 6 out of 6 for Mus81

Category restricted to ProteinDomain (x)

0.019s

Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: Budding yeast Mus81 complexes with Mms4 (EME1 or EME2 in humans) to form a structure-specific endonuclease that targets branched DNA structures with a 5'-end at the branch nick [, ]. Its typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions [, ].Similar to MUS81-EME1, human MUS81-EME2 cleaves 3'-flaps, replication forks and nicked Holliday junctions, and exhibits limited endonuclease activity with intact Holliday junctions. However, MUS81-EME2 can also cleave a variety of DNA structures including D-loop recombination intermediates and nicked duplex [, ].
Protein Domain
Type: Domain
Description: This entry represents a structural domain found in several DNA repair nucleases, such as Rad1, XPF and crossover junction endonucleases EME1 and Mus81 [, ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases.
Protein Domain
Type: Homologous_superfamily
Description: This superfamily includes the C-terminal domain found in Eme1 from fission yeasts, and EME1/EME2 from animals. They interact with Mus81 to from a complex, which acts as a structure-specific endonuclease that targets branched DNA structures with a 5'-end at the branch nick [, ]. The typical substrates of this complex include 3'-flap structures, replication forks and nicked Holliday junctions [, ].Similar to MUS81-EME1, human MUS81-EME2 cleaves 3'-flaps, replication forks and nicked Holliday junctions, and exhibits limited endonuclease activity with intact Holliday junctions. However, MUS81-EME2 can also cleave a variety of DNA structures including D-loop recombination intermediates and nicked duplex [, ].Both Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix [].
Protein Domain
Type: Homologous_superfamily
Description: The Mus81-Eme1 complex is a structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the meiotic recombination intermediates in eukaryotes. Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix.The nuclease domain is found in several DNA repair nucleases, including Rad1, XPF and crossover junction endonucleases EME1 (an essential component of a Holliday junction resolvase) and Mus81 [, ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases.This superfamily consists of the second subdomain of the nuclease domain found in EME1.
Protein Domain
Type: Homologous_superfamily
Description: The Mus81-Eme1 complex is a structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the meiotic recombination intermediates in eukaryotes. Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix.The nuclease domain is found in several DNA repair nucleases, including Rad1, XPF and crossover junction endonucleases EME1 (an essential component of a Holliday junction resolvase) and Mus81 [, ]. The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases.This superfamily consists of the first part of the nuclease domain found in EME1.
Protein Domain
Type: Family
Description: This entry includes Mms4 from budding yeast, Eme1 from fission yeasts, and EME1/EME2 from animals. They interact with Mus81 to from a complex, which acts as a structure-specific endonuclease that targets branched DNA structures with a 5'-end at the branch nick [, ]. The typical substrates of this complex include 3'-flap structures, replication forks and nicked Holliday junctions [, ].Similar to MUS81-EME1, human MUS81-EME2 cleaves 3'-flaps, replication forks and nicked Holliday junctions, and exhibits limited endonuclease activity with intact Holliday junctions. However, MUS81-EME2 can also cleave a variety of DNA structures including D-loop recombination intermediates and nicked duplex [, ].