The formation of centromeric chromatin assembly outside the context of DNA replication involves the assembly of nucleosomes containing the histone H3 variant CenH3 (also called CENP-A).
Foltz DR, Jansen LE, Black BE, Bailey AO, Yates JR, Cleveland DW.; ''The human CENP-A centromeric nucleosome-associated complex.''; PubMedEurope PMCScholia
Foltz DR, Jansen LE, Bailey AO, Yates JR, Bassett EA, Wood S, Black BE, Cleveland DW.; ''Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP.''; PubMedEurope PMCScholia
Obuse C, Yang H, Nozaki N, Goto S, Okazaki T, Yoda K.; ''Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase.''; PubMedEurope PMCScholia
Barnhart MC, Kuich PH, Stellfox ME, Ward JA, Bassett EA, Black BE, Foltz DR.; ''HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore.''; PubMedEurope PMCScholia
Dunleavy EM, Roche D, Tagami H, Lacoste N, Ray-Gallet D, Nakamura Y, Daigo Y, Nakatani Y, Almouzni-Pettinotti G.; ''HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres.''; PubMedEurope PMCScholia
Shuaib M, Ouararhni K, Dimitrov S, Hamiche A.; ''HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres.''; PubMedEurope PMCScholia
Perpelescu M, Nozaki N, Obuse C, Yang H, Yoda K.; ''Active establishment of centromeric CENP-A chromatin by RSF complex.''; PubMedEurope PMCScholia
Carroll CW, Silva MC, Godek KM, Jansen LE, Straight AF.; ''Centromere assembly requires the direct recognition of CENP-A nucleosomes by CENP-N.''; PubMedEurope PMCScholia
Okada M, Cheeseman IM, Hori T, Okawa K, McLeod IX, Yates JR, Desai A, Fukagawa T.; ''The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres.''; PubMedEurope PMCScholia
Fujita Y, Hayashi T, Kiyomitsu T, Toyoda Y, Kokubu A, Obuse C, Yanagida M.; ''Priming of centromere for CENP-A recruitment by human hMis18alpha, hMis18beta, and M18BP1.''; PubMedEurope PMCScholia
Hayashi T, Fujita Y, Iwasaki O, Adachi Y, Takahashi K, Yanagida M.; ''Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres.''; PubMedEurope PMCScholia
Maddox PS, Hyndman F, Monen J, Oegema K, Desai A.; ''Functional genomics identifies a Myb domain-containing protein family required for assembly of CENP-A chromatin.''; PubMedEurope PMCScholia
Carroll CW, Milks KJ, Straight AF.; ''Dual recognition of CENP-A nucleosomes is required for centromere assembly.''; PubMedEurope PMCScholia
The Mis18 complex binds the centromere in late telophase/early G1 phase. The mechanism of interaction between the Mis18 complex and the centromeric core is unknown.
The mechanism of interaction between the CENPH-I Complex and the centromeric nucleosome (containing CENPA) is unknown. The CENH-I complex is observed to interact with the centromeric core throughout the cell cycle.
The HJURP complex binds free, newly synthesized CENPA-H4 tetramers. A direct interaction occurs between HJURP and CENPA. The CATD domain of CENPA is sufficient for the interaction. The complex then localizes to the centromere in early G1 phase. HJURP is required for deposition of new CENPA-containing nucleosomes.
The Mis18 complex (containing Mis18-alpha, Mis18-beta, Mis18BP1, RBap46, and RbAp48) transiently binds the centromere in late anaphase-telophase to early G1. The mechanism by which the Mis18 complex binds the centromere is unknown. The Mis18 complex is required for deposition of new CENPA-containing nucleosomes at the centromere. The CENPH-I complex is constitutively associated with centromeres and is required for deposition of new CENPA-containing nucleosomes.
A new centromeric nucleosome containing histone H2A, histone H2B, histone H4, and CENPA is deposited at the centromere in late telophase/early G1 phase. The exact mechanism by which the new CENPA-containing nucleosome is transferred to DNA is unknown. HJURP directly binds newly synthesized CENPA before deposition. The Mis18 and HJURP complexes are required for deposition of newly synthesized CENPA-containing nucleosomes. The exact stoichiometries and interactions of the complexes are unknown.
The RSF complex binds the centromere in mid-G1 phase after deposition of new CENPA-containing nucleosomes has occurred. The RSF complex is required for stable incorporation of the previously deposited CENPA-containing nucleosomes.
Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=774815
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Mis18
HJURP ComplexCENPH-I
Mis18 ComplexCENPH-I Centromeric Nucleosome
RSF ComplexCENPH-I Mis18 HJURP
CENPA ComplexAnnotated Interactions
CENPH-I
Mis18 ComplexCENPH-I Centromeric Nucleosome
RSF ComplexCENPH-I Mis18 HJURP
CENPA Complex