期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 281, 期 48, 页码 36952-36959出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M608004200
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资金
- Biotechnology and Biological Sciences Research Council [BB/D522746/1] Funding Source: Medline
- Cancer Research UK [A5451] Funding Source: Medline
- Medical Research Council [G0501450] Funding Source: Medline
- MRC [G0501450] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D522746/1] Funding Source: researchfish
- Medical Research Council [G0300662B, G0501450] Funding Source: researchfish
Structural maintenance of chromosomes (SMC) proteins play fundamental roles in many aspects of chromosome organization and dynamics. The SMC complexes form unique structures with long coiled-coil arms folded at a hinge domain, so that the globular N-and C-terminal domains are brought together to form a head. Within the Smc5-Smc6 complex, we previously identified two subcomplexes containing Smc6-Smc5-Nse2 and Nse1-Nse3-Nse4. A third subcomplex containing Nse5 and -6 has also been identified recently. We present evidence that Nse4 is the kleisin component of the complex, which bridges the heads of Smc5 and -6. The C-terminal part of Nse4 interacts with the head domain of Smc5, and structural predictions for Nse4 proteins suggest similar motifs that are shared within the kleisin family. Specific mutations within a predicted winged helix motif of Nse4 destroy the interaction with Smc5. We propose that Nse4 and its orthologs form the delta-kleisin subfamily. We further show that Nse3, as well as Nse5 and Nse6, also bridge the heads of Smc5 and -6. The Nse1-Nse3-Nse4 and Nse5-Nse6 subcomplexes bind to the Smc5-Smc6 heads domain at different sites.
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