This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The structural maintenance of chromosome (SMC) proteins, which are evolutionarily conserved from prokaryotes to eukaryotes, is essential for higher-order chromosome organizations and functions. Six members of SMCs have been found in eukaryotes, from SMC1 to SMC6, which form three distinct complexes, each with a unique function. SMC5 and SMC6 interact with each other and associate with non-SMC elements to form the SMC5-6 complex that is essential for both DNA replication and the repair of DNA damage. Under normal conditions, SMC5-6 is located at repetitive rDNA and telomere and responses for DNA replication and thus for cell survival. In addition, when DNA is damaged by UV radiation or DNA damage reagents, SMC5-6 is translocated to the DNA damage site as a response to DNA damage repair. SMC proteins are organized into five domains: an N-terminal head domain, a long coiled-coil helix, a hinge domain, another long coiled-coil helix and a C-terminal head domain. The N- and C-terminal head domains associate together to form an ATPase head domain. The long coiled-coil helices associate together to form the coiled-coil arm. The hinge domain dimerizes to form the hinge of the complex. The size and overall conformation of the SMC complexes make the study of the full-length proteins by crystallographic analysis difficult. However, the SMC proteins have conserved domains that can be assembled independently, suggesting that it will be possible to examine the structure of the individual domains and glean information on how structural changes in these conserved domains are linked to discrete functions for the different SMC family members.
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