Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex
Journal of Molecular Biology , Volume 339 - Issue 4 p. 937- 949
Structural maintenance of chromosomes (SMC) proteins have diverse cellular functions including chromosome segregation, condensation and DNA repair. They are grouped based on a conserved set of distinct structural motifs. All SMC proteins are predicted to have a bipartite ATPase domain that is separated by a long region predicted to form a coiled coil. Recent structural data on a variety of SMC proteins shows them to be arranged as long intramolecular coiled coils with a globular ATPase at one end. SMC proteins function in pairs as heterodimers or as homodimers often in complexes with other proteins. We expect the arrangement of the SMC protein domains in complex assemblies to have important implications for their diverse functions. We used scanning force microscopy imaging to determine the architecture of human, Saccharomyces cerevisiae, and Pyrococcus furiosus Rad50/Mre11, Escherichia coli SbcCD, and S.cerevisiae SMC1/SMC3 cohesin SMC complexes. Two distinct architectural arrangements are described, based on the way their components were connected. The eukaryotic complexes were similar to each other and differed from their prokaryotic and archaeal homologs. These similarities and differences are discussed with respect to their diverse mechanistic roles in chromosome metabolism.
|DNA metabolism, protein architecture, SbcCD, scanning force microscopy (SFM), SFM, scanning force microscopy, SMC, structural maintenance of chromosomes, structural maintenance of chromosomes (SMC)|
|Journal of Molecular Biology|
|Organisation||Department of Molecular Genetics|
de Jager, M, Wyman, C, Trujillo, J.P, Sung, P, Hopfner, K.-P, Carney, J.P, … Kanaar, R. (2004). Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex. Journal of Molecular Biology, 339(4), 937–949. doi:10.1016/j.jmb.2004.04.014