Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5
Cohesin organizes DNA into chromatids, regulates enhancer-promoter interactions, and confers sister chromatid cohesion. Its association with chromosomes is regulated by hook-shaped HEAT repeat proteins that bind Scc1, namely Scc3, Pds5, and Scc2. Unlike Pds5, Scc2 is not a stable cohesin constituent...
| Main Authors: | , , , , , , , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
Elsevier
2018
|
| _version_ | 1797067723988008960 |
|---|---|
| author | Petela, N Gligoris, T Metson, J Lee, B Voulgaris, M Hu, B Kikuchi, S Chapard, C Chen, W Rajendra, E Srinivisan, M Yu, H Löwe, J Nasmyth, K |
| author_facet | Petela, N Gligoris, T Metson, J Lee, B Voulgaris, M Hu, B Kikuchi, S Chapard, C Chen, W Rajendra, E Srinivisan, M Yu, H Löwe, J Nasmyth, K |
| author_sort | Petela, N |
| collection | OXFORD |
| description | Cohesin organizes DNA into chromatids, regulates enhancer-promoter interactions, and confers sister chromatid cohesion. Its association with chromosomes is regulated by hook-shaped HEAT repeat proteins that bind Scc1, namely Scc3, Pds5, and Scc2. Unlike Pds5, Scc2 is not a stable cohesin constituent but, as shown here, transiently replaces Pds5. Scc1 mutations that compromise its interaction with Scc2 adversely affect cohesin's ATPase activity and loading. Moreover, Scc2 mutations that alter how the ATPase responds to DNA abolish loading despite cohesin's initial association with loading sites. Lastly, Scc2 mutations that permit loading in the absence of Scc4 increase Scc2's association with chromosomal cohesin and reduce that of Pds5. We suggest that cohesin switches between two states: one with Pds5 bound that is unable to hydrolyze ATP efficiently but is capable of release from chromosomes and another in which Scc2 replaces Pds5 and stimulates ATP hydrolysis necessary for loading and translocation from loading sites. |
| first_indexed | 2024-03-06T22:00:24Z |
| format | Journal article |
| id | oxford-uuid:4e61e11b-9c8c-4e6b-b33f-ebe7214ff2e8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:00:24Z |
| publishDate | 2018 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:4e61e11b-9c8c-4e6b-b33f-ebe7214ff2e82022-03-26T16:00:56ZScc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4e61e11b-9c8c-4e6b-b33f-ebe7214ff2e8EnglishSymplectic Elements at OxfordElsevier2018Petela, NGligoris, TMetson, JLee, BVoulgaris, MHu, BKikuchi, SChapard, CChen, WRajendra, ESrinivisan, MYu, HLöwe, JNasmyth, KCohesin organizes DNA into chromatids, regulates enhancer-promoter interactions, and confers sister chromatid cohesion. Its association with chromosomes is regulated by hook-shaped HEAT repeat proteins that bind Scc1, namely Scc3, Pds5, and Scc2. Unlike Pds5, Scc2 is not a stable cohesin constituent but, as shown here, transiently replaces Pds5. Scc1 mutations that compromise its interaction with Scc2 adversely affect cohesin's ATPase activity and loading. Moreover, Scc2 mutations that alter how the ATPase responds to DNA abolish loading despite cohesin's initial association with loading sites. Lastly, Scc2 mutations that permit loading in the absence of Scc4 increase Scc2's association with chromosomal cohesin and reduce that of Pds5. We suggest that cohesin switches between two states: one with Pds5 bound that is unable to hydrolyze ATP efficiently but is capable of release from chromosomes and another in which Scc2 replaces Pds5 and stimulates ATP hydrolysis necessary for loading and translocation from loading sites. |
| spellingShingle | Petela, N Gligoris, T Metson, J Lee, B Voulgaris, M Hu, B Kikuchi, S Chapard, C Chen, W Rajendra, E Srinivisan, M Yu, H Löwe, J Nasmyth, K Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5 |
| title | Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5 |
| title_full | Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5 |
| title_fullStr | Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5 |
| title_full_unstemmed | Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5 |
| title_short | Scc2 is a potent activator of Cohesin’s ATPase that promotes loading by binding Scc1 without Pds5 |
| title_sort | scc2 is a potent activator of cohesin s atpase that promotes loading by binding scc1 without pds5 |
| work_keys_str_mv | AT petelan scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT gligorist scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT metsonj scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT leeb scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT voulgarism scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT hub scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT kikuchis scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT chapardc scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT chenw scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT rajendrae scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT srinivisanm scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT yuh scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT lowej scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 AT nasmythk scc2isapotentactivatorofcohesinsatpasethatpromotesloadingbybindingscc1withoutpds5 |