Kite Proteins: a Superfamily of SMC/Kleisin Partners Conserved Across Bacteria, 
Archaea, and Eukaryotes

Palecek, Jan J.; Gruber, Stephan

doi:10.1016/j.str.2015.10.004

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Kite Proteins: a Superfamily of SMC/Kleisin Partners Conserved Across Bacteria, Archaea, and Eukaryotes

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Gruber, Stephan
Gruber, Stephan / Chromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Palecek, J. J., & Gruber, S. (2015). Kite Proteins: a Superfamily of SMC/Kleisin Partners Conserved Across Bacteria, Archaea, and Eukaryotes. STRUCTURE, 23(12), 2183-2190. doi:10.1016/j.str.2015.10.004.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-5B59-B

Abstract

SMC/kleisin complexes form elongated annular structures, which are critical for chromosome segregation, genome maintenance, and the regulation of gene expression. We describe marked structural similarities between bacterial and eukaryotic SMC/kleisin partner proteins (designated here as "kite'' proteins for kleisin interacting tandem winged-helix (WH) elements of SMC complexes). Kite proteins are integral parts of all prokaryotic SMC complexes and Smc5/6 but not cohesin and condensin. They are made up of tandem WH domains, form homo-or heterodimers via their amino-terminal WH domain, and they associate with the central part of a kleisin subunit. In placental mammals, the kite subunit NSE3 gave rise to several (>60) kite-related proteins, named MAGE, many of which encode tumor-and testis-specific antigens. Based on architectural rather than sequence similarity, we propose an adapted model for the evolution of the SMC protein complexes and discuss potential functional similarities between bacterial Smc/ScpAB and eukaryotic Smc5/6.