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From Proteopedia
Crystal structure of human MUS81-EME2 complex
Structural highlights
FunctionMUS81_HUMAN Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedMUS81 is an important structure-specific endonuclease responsible for the processing of stalled replication forks and recombination intermediates. In human, MUS81 functions by forming complexes with its regulatory subunits EME1 and EME2, playing distinct roles in G2/M and S phases. Although the structures of MUS81-EME1 have been intensively studied, there is no structure information available about MUS81-EME2. Here, we report the crystal structure of MUS81-EME2, which reveals an overall protein fold similar to that of MUS81-EME1 complex. Further biochemical and structural characterization shows that the MUS81-EME1 and MUS81-EME2 complexes are identical in substrate recognition and endonuclease activities in vitro, implying that the distinct cellular roles of the two complexes could arise from temporal controls in cells. Finally, an extensive structure-guided mutagenesis analysis provides implications for the molecular basis of how the MUS81-EME endonucleases recognize various DNA substrates in a structure-selective manner. Crystal structure of the human MUS81-EME2 complex.,Hua Z, Fang Q, Zhang D, Luo Z, Yuan C, Lin Z Structure. 2022 May 5;30(5):743-752.e3. doi: 10.1016/j.str.2022.02.015. Epub 2022 , Mar 14. PMID:35290797[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Hua ZK | Lin ZH | Yuan C | Zhang DP
