期刊
STRUCTURE
卷 23, 期 12, 页码 2183-2190出版社
CELL PRESS
DOI: 10.1016/j.str.2015.10.004
关键词
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资金
- Max Planck Society
- ERC [260853]
- Czech Science Foundation [GA13-00774S]
- European Regional Development Fund [CZ.1.05/1.1.00/02.0068]
- European Research Council (ERC) [260853] Funding Source: European Research Council (ERC)
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.
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