Structural Insights into Ring Formation of Cohesin and Related Smc Complexes

• Published in: Trends in cell biology Vol. 26; no. 9; pp. 680 - 693
• Main Authors: Gligoris, Thomas, Löwe, Jan
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.09.2016; Elsevier Science Publishers
• Subjects: Animals; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - metabolism; Chromatids - metabolism; Chromosomal Proteins, Non-Histone - chemistry; Chromosomal Proteins, Non-Histone - metabolism; Cohesins; Eukaryotic Cells - metabolism; Humans; Models, Biological; Multiprotein Complexes - metabolism; Pathology; Review
• ISSN: 0962-8924; 1879-3088
• DOI: 10.1016/j.tcb.2016.04.002

Cohesin facilitates sister chromatid cohesion through the formation of a large ring structure that encircles DNA. Its function relies on two structural maintenance of chromosomes (Smc) proteins, which are found in almost all organisms tested, from bacteria to humans. In accordance with their ubiquity, Smc complexes, such as cohesin, condensin, Smc5-6, and the dosage compensation complex, affect almost all processes of DNA homeostasis. Although their precise molecular mechanism remains enigmatic, here we provide an overview of the architecture of eukaryotic Smc complexes with a particular focus on cohesin, which has seen the most progress recently. Given the evident conservation of many structural features between Smc complexes, it is expected that architecture and topology will have a significant role when deciphering their precise molecular mechanisms.