TY - JOUR
T1 - Association of M18BP1/KNL2 with CENP-A Nucleosome Is Essential for Centromere Formation in Non-mammalian Vertebrates
AU - Hori, Tetsuya
AU - Shang, Wei Hao
AU - Hara, Masatoshi
AU - Ariyoshi, Mariko
AU - Arimura, Yasuhiro
AU - Fujita, Risa
AU - Kurumizaka, Hitoshi
AU - Fukagawa, Tatsuo
PY - 2017/7/24
Y1 - 2017/7/24
N2 - Centromeres are specified and maintained by sequence-independent epigenetic mechanisms through the incorporation of CENP-A into centromeres. Given that CENP-A incorporation requires the Mis18 complex to be in the centromere region, it is necessary to precisely understand how the Mis18 complex localizes to the centromere region. Here, we showed that centromere localization of the Mis18 complex depends on CENP-A, but not CENP-C or CENP-T, in chicken DT40 cells. Furthermore, we demonstrated that M18BP1/KNL2, a member of the Mis18 complex, contained the CENP-C-like motif in chicken and other vertebrates, which is essential for centromere localization and M18BP1/KNL2 function in DT40 cells. We also showed that in vitro reconstituted CENP-A nucleosome, but not H3 nucleosome, bound to the CENP-C-like motif containing M18BP1/KNL2. Based on these results, we conclude that M18BP1/KNL2 is essential for centromere formation through direct binding to CENP-A nucleosome in non-mammalian vertebrates. This explains how new CENP-A recognizes the centromere position. Centromeres are specified and maintained by the incorporation of the histone H3 variant CENP-A. Hori at al. provide insight into how new CENP-A recognizes the centromere position in non-mammalian vertebrates and demonstrate that the association of M18BP1/KNL2, a Mis18 complex component, with CENP-A nucleosome is essential for centromere formation.
AB - Centromeres are specified and maintained by sequence-independent epigenetic mechanisms through the incorporation of CENP-A into centromeres. Given that CENP-A incorporation requires the Mis18 complex to be in the centromere region, it is necessary to precisely understand how the Mis18 complex localizes to the centromere region. Here, we showed that centromere localization of the Mis18 complex depends on CENP-A, but not CENP-C or CENP-T, in chicken DT40 cells. Furthermore, we demonstrated that M18BP1/KNL2, a member of the Mis18 complex, contained the CENP-C-like motif in chicken and other vertebrates, which is essential for centromere localization and M18BP1/KNL2 function in DT40 cells. We also showed that in vitro reconstituted CENP-A nucleosome, but not H3 nucleosome, bound to the CENP-C-like motif containing M18BP1/KNL2. Based on these results, we conclude that M18BP1/KNL2 is essential for centromere formation through direct binding to CENP-A nucleosome in non-mammalian vertebrates. This explains how new CENP-A recognizes the centromere position. Centromeres are specified and maintained by the incorporation of the histone H3 variant CENP-A. Hori at al. provide insight into how new CENP-A recognizes the centromere position in non-mammalian vertebrates and demonstrate that the association of M18BP1/KNL2, a Mis18 complex component, with CENP-A nucleosome is essential for centromere formation.
KW - CENP-A
KW - centromere specification
KW - epigenetics
KW - kinetochore
KW - M18BP1/KNL2
KW - Mis18 complex
UR - http://www.scopus.com/inward/record.url?scp=85024389437&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85024389437&partnerID=8YFLogxK
U2 - 10.1016/j.devcel.2017.06.019
DO - 10.1016/j.devcel.2017.06.019
M3 - Article
C2 - 28743004
AN - SCOPUS:85024389437
SN - 1534-5807
VL - 42
SP - 181-189.e3
JO - Developmental Cell
JF - Developmental Cell
IS - 2
ER -