Research Article

Cryo-EM structure of the human cohesin-NIPBL-DNA complex

See allHide authors and affiliations

Science  26 Jun 2020:
Vol. 368, Issue 6498, pp. 1454-1459
DOI: 10.1126/science.abb0981

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

A blueprint to understand cohesin

Cohesin is a multiprotein complex that entraps sister chromatids for chromosome segregation and regulates transcription by extruding DNA loops to shape DNA organization. Shi et al. determined the structure of human cohesin bound to the protein NIBPL, which helps load cohesin onto DNA, and DNA at medium resolution by cryo–electron microscopy. Two adenosine triphosphatase domains play a key role in cohesin function. The structure explains how NIBPL and DNA synergistically activate these domains and gives insight into how DNA is trapped by cohesin.

Science, this issue p. 1454


As a ring-shaped adenosine triphosphatase (ATPase) machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo–electron microscopy (cryo-EM), we determined the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72–base pair DNA. NIPBL and DNA promote the engagement of cohesin’s ATPase head domains and ATP binding. The hinge domains of cohesin adopt an “open washer” conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA and provides insight into DNA entrapment by cohesin.

View Full Text

Stay Connected to Science