CENP-A chromatin forms the foundation for kinetochore assembly. 
Replication-independent incorporation of CENP-A at centromeres depends on its 
chaperone HJURP(Scm3), and Mis18 in vertebrates and fission yeast. The 
recruitment of Mis18 and HJURP(Scm3) to centromeres is cell cycle regulated. 
Vertebrate Mis18 associates with Mis18BP1(KNL2), which is critical for the 
recruitment of Mis18 and HJURP(Scm3). We identify two novel fission yeast 
Mis18-interacting proteins (Eic1 and Eic2), components of the Mis18 complex. 
Eic1 is essential to maintain Cnp1(CENP-A) at centromeres and is crucial for 
kinetochore integrity; Eic2 is dispensable. Eic1 also associates with 
Fta7(CENP-Q/Okp1), Cnl2(Nkp2) and Mal2(CENP-O/Mcm21), components of the 
constitutive CCAN/Mis6/Ctf19 complex. No Mis18BP1(KNL2) orthologue has been 
identified in fission yeast, consequently it remains unknown how the key 
Cnp1(CENP-A) loading factor Mis18 is recruited. Our findings suggest that Eic1 
serves a function analogous to that of Mis18BP1(KNL2), thus representing the 
functional counterpart of Mis18BP1(KNL2) in fission yeast that connects with a 
module within the CCAN/Mis6/Ctf19 complex to allow the temporally regulated 
recruitment of the Mis18/Scm3(HJURP) Cnp1(CENP-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.