Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly
CENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURPScm3, and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURPScm3 to centromeres is cell cycle regulated. Vertebrate Mis...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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The Royal Society
2014-01-01
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| Series: | Open Biology |
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| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140043 |
| _version_ | 1819038693068898304 |
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| author | Lakxmi Subramanian Nicholas R. T. Toda Juri Rappsilber Robin C. Allshire |
| author_facet | Lakxmi Subramanian Nicholas R. T. Toda Juri Rappsilber Robin C. Allshire |
| author_sort | Lakxmi Subramanian |
| collection | DOAJ |
| description | CENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURPScm3, and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURPScm3 to centromeres is cell cycle regulated. Vertebrate Mis18 associates with Mis18BP1KNL2, which is critical for the recruitment of Mis18 and HJURPScm3. We identify two novel fission yeast Mis18-interacting proteins (Eic1 and Eic2), components of the Mis18 complex. Eic1 is essential to maintain Cnp1CENP-A at centromeres and is crucial for kinetochore integrity; Eic2 is dispensable. Eic1 also associates with Fta7CENP-Q/Okp1, Cnl2Nkp2 and Mal2CENP-O/Mcm21, components of the constitutive CCAN/Mis6/Ctf19 complex. No Mis18BP1KNL2 orthologue has been identified in fission yeast, consequently it remains unknown how the key Cnp1CENP-A loading factor Mis18 is recruited. Our findings suggest that Eic1 serves a function analogous to that of Mis18BP1KNL2, thus representing the functional counterpart of Mis18BP1KNL2 in fission yeast that connects with a module within the CCAN/Mis6/Ctf19 complex to allow the temporally regulated recruitment of the Mis18/Scm3HJURP Cnp1CENP-A loading factors. The novel interactions identified between CENP-A loading factors and the CCAN/Mis6/Ctf19 complex are likely to also contribute to CENP-A maintenance in other organisms. |
| first_indexed | 2024-12-21T08:41:22Z |
| format | Article |
| id | doaj.art-e0127d6c23514bc6bbd381fcff119361 |
| institution | Directory Open Access Journal |
| issn | 2046-2441 |
| language | English |
| last_indexed | 2024-12-21T08:41:22Z |
| publishDate | 2014-01-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj.art-e0127d6c23514bc6bbd381fcff1193612022-12-21T19:09:57ZengThe Royal SocietyOpen Biology2046-24412014-01-014410.1098/rsob.140043140043Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assemblyLakxmi SubramanianNicholas R. T. TodaJuri RappsilberRobin C. AllshireCENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURPScm3, and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURPScm3 to centromeres is cell cycle regulated. Vertebrate Mis18 associates with Mis18BP1KNL2, which is critical for the recruitment of Mis18 and HJURPScm3. We identify two novel fission yeast Mis18-interacting proteins (Eic1 and Eic2), components of the Mis18 complex. Eic1 is essential to maintain Cnp1CENP-A at centromeres and is crucial for kinetochore integrity; Eic2 is dispensable. Eic1 also associates with Fta7CENP-Q/Okp1, Cnl2Nkp2 and Mal2CENP-O/Mcm21, components of the constitutive CCAN/Mis6/Ctf19 complex. No Mis18BP1KNL2 orthologue has been identified in fission yeast, consequently it remains unknown how the key Cnp1CENP-A loading factor Mis18 is recruited. Our findings suggest that Eic1 serves a function analogous to that of Mis18BP1KNL2, thus representing the functional counterpart of Mis18BP1KNL2 in fission yeast that connects with a module within the CCAN/Mis6/Ctf19 complex to allow the temporally regulated recruitment of the Mis18/Scm3HJURP Cnp1CENP-A loading factors. The novel interactions identified between CENP-A loading factors and the CCAN/Mis6/Ctf19 complex are likely to also contribute to CENP-A maintenance in other organisms.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140043cenp-acentromeresepigeneticsfission yeastmis18 |
| spellingShingle | Lakxmi Subramanian Nicholas R. T. Toda Juri Rappsilber Robin C. Allshire Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly Open Biology cenp-a centromeres epigenetics fission yeast mis18 |
| title | Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly |
| title_full | Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly |
| title_fullStr | Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly |
| title_full_unstemmed | Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly |
| title_short | Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly |
| title_sort | eic1 links mis18 with the ccan mis6 ctf19 complex to promote cenp a assembly |
| topic | cenp-a centromeres epigenetics fission yeast mis18 |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140043 |
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