Structural Basis and IP6 Requirement for Pds5-Dependent Cohesin Dynamics.
Mol Cell
; 62(2): 248-259, 2016 04 21.
Article
in En
| MEDLINE
| ID: mdl-26971492
ABSTRACT
The ring-shaped cohesin complex regulates transcription, DNA repair, and chromosome segregation by dynamically entrapping chromosomes to promote chromosome compaction and sister-chromatid cohesion. The cohesin ring needs to open and close to allow its loading to and release from chromosomes. Cohesin dynamics are controlled by the releasing factors Pds5 and Wapl and the cohesin stabilizer Sororin. Here, we report the crystal structure of human Pds5B bound to a conserved peptide motif found in both Wapl and Sororin. Our structure establishes the basis for how Wapl and Sororin antagonistically influence cohesin dynamics. The structure further reveals that Pds5 can bind inositol hexakisphosphate (IP6). The IP6-binding segment of Pds5B is shaped like the jaw of a plier lever and inhibits the binding of Scc1 to Smc3. We propose that Pds5 stabilizes a transient, open state of cohesin to promote its release from chromosomes.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phytic Acid
/
Transcription Factors
/
Chromosomal Proteins, Non-Histone
/
Chromosomes, Human
/
Cell Cycle Proteins
/
DNA-Binding Proteins
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
Mol Cell
Journal subject:
BIOLOGIA MOLECULAR
Year:
2016
Type:
Article
Affiliation country:
United States