Molecular basis for CENP-N recognition of CENP-A nucleosome on the human kinetochore

Tian, Tian; Li, Xiaorun; Liu, Yingying; Wang, Chengliang; Liu, Xing; Bi, Guo-Qiang; Zhang, Xuan; Yao, Xuebiao; Zhou, Z. Hong; Zang, Jianye

doi:10.1038/cr.2018.13

Cited by 73 publications

(91 citation statements)

References 10 publications

(13 reference statements)

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“…Interestingly, our EMSA and XLMS data suggest that in contrast to the human ortholog, CENP-N/L, the Chl4/Iml3 heterodimer does not directly interact with Cse4-NCP, but is linked to Ame1/Okp1 and Mif2 (Figure 1A, C). Recent electron microscopy reconstructions of human CENP-A nucleosomes in complex with CENP-N/L identified the RG loop in the CATD (Zhou et al, 2011) to be required for CENP-N interacting with CENP-A (Chittori et al, 2018, Pentakota et al, 2017, Tian et al, 2018. The lack of this RG loop in the budding yeast Cse4 CATD is consistent with our finding of Chl4/Iml3 being positioned distal from Cse4 nucleosomes ( Figure 1A, C).…”

Section: Dual Recognition Of Cse4 At Point Centromeres By a Ccan Archsupporting

confidence: 88%

“…Across different species the CENP-C signature motif interacts with divergent hydrophobic residues of the CENP-A C-terminal tail (Musacchio and Desai, 2017). Electron microscopy studies have recently resolved the interaction of CENP-N with the CENP-A centromere-targeting domain (CATD) of CENP-A-NCP in vertebrates (Carroll et al, 2009, Guse et al, 2011, Pentakota et al, 2017, Chittori et al, 2018, Tian et al, 2018. For budding yeast Cse4 a direct interaction has so far only been demonstrated with Mif2 (Westermann et al, 2003, Xiao et al, 2017.…”

Section: Introductionmentioning

confidence: 99%

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The COMA complex is required for positioning Ipl1 activity proximal to Cse4 nucleosomes in budding yeast

Fischboeck

Singh

Potocnjak

et al. 2018

Preprint

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Kinetochores are macromolecular protein complexes assembled on centromeric chromatin that ensure accurate chromosome segregation by linking DNA to spindle microtubules and integrating safeguard mechanisms. A kinetochore-associated pool of Ipl1 Aurora B kinase, a subunit of the chromosomal passenger complex (CPC), was previously implicated in feedback control mechanisms. To study the kinetochore subunit connectivity built on budding yeast point centromeres and its CPC interactions we performed crosslink-guided in vitro reconstitution. The Ame1/Okp1 CENP-U/Q heterodimer, forming the COMA complex with Ctf19/Mcm21 CENP-P/O , selectively bound Cse4 CENP-A nucleosomes through the Cse4 N-terminus and thereby establishes a direct link to the outer kinetochore MTW1 complex. The Sli15/Ipl1 INCENP/Aurora B core-CPC interacted with COMA through the Ctf19 C-terminus, and artificial tethering of Sli15 to Ame1/Okp1 rescued synthetic lethality upon Ctf19/Mcm21 deletion in a Sli15 centromeretargeting deficient mutant. This study reveals characteristics of the inner kinetochore architecture assembled at point centromeres and the relevance of its Sli15/Ipl1 interaction for CPC function.

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Section: Dual Recognition Of Cse4 At Point Centromeres By a Ccan Archsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

The COMA complex is required for positioning Ipl1 activity proximal to Cse4 nucleosomes in budding yeast

Fischboeck

Singh

Potocnjak

et al. 2018

Preprint

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“…Crystal structure of CENP-A nucleosome (Tachiwana et al, 2011), in vivo MNase experiments (Hasson et al, 2013) and initial cryoEM studies (Roulland et al, 2016) Next most intriguing question is how CENP-A nucleosome directly binds 2 CCAN components, CENP-N and CENP-C, and how is their binding changing the nucleosome. Recent work (Chittori et al, 2018;Pentakota et al, 2017;Tian et al, 2018) provides the atomic resolution view at CENP-A/CENP-N interaction, which involves recognition of the solvent-exposed L1 loop on CENP-A and interaction with DNA, but structure of CENP-A nucleosome in complex with CENP-C is still missing. Currently, 2 different parts of CENP-C are proposed to bind CENP-A nucleosome: CENP-C CR and CENP-C motif .…”

Section: Discussionmentioning

confidence: 99%

“…Initial clues came from the crystal structure of the CENP-A nucleosome (Tachiwana et al, 2011) that implied octameric histone core, similar to canonical nucleosome, with unwrapped DNA ends. Recently, a cryoEM structure of the human CENP-A nucleosome in complex with human CENP-N has been reported by several groups (Chittori et al, 2018;Pentakota et al, 2017;Tian et al, 2018) revealing high-resolution molecular determinants for the CENP-A/CENP-N interaction. However, high-resolution structure of human CENP-A nucleosome in complex with CENP-C is still missing.…”

Section: Introductionmentioning

confidence: 99%

CENP-C unwraps the CENP-A nucleosome through the H2A C-terminal tail

Ali-Ahmad

Bilokapić

Schäfer

et al. 2019

Preprint

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Centromere is a chromosome locus necessary for genetic stability during cell division.Centromere is defined epigenetically, by nucleosome containing histone H3 variant, CENP-A, upon which constitutive centromere-associated network of proteins (CCAN) is built. CENP-C, a member of CCAN, is considered to be a blueprint of centromere. It interacts with several CCAN components and directly bridges CENP-A nucleosomes to kinetochore in mitosis. In this study, we provide new molecular details on structure

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“…CENP-C, a CCAN component, is a key hub protein for kinetochore assembly (Fukagawa and Brown, 1997; Fukagawa et al, 1999; Klare et al, 2015; Kwon et al, 2007; Saitoh et al, 1992; Weir et al, 2016). CENP-C has multifunctional domains that bind to various proteins, including the Mis12 complex (Dimitrova et al, 2016; Petrovic et al, 2010, 2016; Przewloka et al, 2011), the CENP-L–CENP-N complex (Chittori et al, 2018; McKinley et al, 2015; Nagpal et al, 2015; Pentakota et al, 2017; Tian et al, 2018), the CENP-H–CENP-I–CENP-K–CENP-M complex (CENP-H complex; Basilico et al, 2014; Klare et al, 2015), CENP-B (Fachinetti et al, 2015), and the CENP-A nucleosome (Fachinetti et al, 2013; Falk et al, 2015; Guo et al, 2017; Kato et al, 2013). Previous studies using chicken (gCENP-C) and human CENP-C (hCENP-C) demonstrated that the middle region associates with the CENP-L–CENP-N and CENP-H complexes, and the C-terminal region binds to the CENP-A nucleosome (Klare et al, 2015; McKinley et al, 2015; Nagpal et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization

Watanabe

Hara

Okumura

et al. 2019

Journal of Cell Biology

119

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The kinetochore is essential for faithful chromosome segregation during mitosis. To form a functional kinetochore, constitutive centromere-associated network (CCAN) proteins are assembled on the centromere chromatin that contains the centromere-specific histone CENP-A. CENP-C, a CCAN protein, directly interacts with the CENP-A nucleosome to nucleate the kinetochore structure. As CENP-C is a hub protein for kinetochore assembly, it is critical to address how the CENP-A–CENP-C interaction is regulated during cell cycle progression. To address this question, we investigated the CENP-C C-terminal region, including a conserved CENP-A–binding motif, in both chicken and human cells and found that CDK1-mediated phosphorylation of CENP-C facilitates its binding to CENP-A in vitro and in vivo. We observed that CENP-A binding is involved in CENP-C kinetochore localization during mitosis. We also demonstrate that the CENP-A–CENP-C interaction is critical for long-term viability in human RPE-1 cells. These results provide deeper insights into protein-interaction network plasticity in centromere proteins during cell cycle progression.

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Molecular basis for CENP-N recognition of CENP-A nucleosome on the human kinetochore

Cited by 73 publications

References 10 publications

The COMA complex is required for positioning Ipl1 activity proximal to Cse4 nucleosomes in budding yeast

The COMA complex is required for positioning Ipl1 activity proximal to Cse4 nucleosomes in budding yeast

CENP-C unwraps the CENP-A nucleosome through the H2A C-terminal tail

CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization

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