The structure of the yeast Ctf3 complex

Hinshaw, Stephen M.; Dates, Andrew N.

doi:10.7554/elife.48215

Cited by 19 publications

(22 citation statements)

References 39 publications

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“…Major recent progress has been made in understanding the structure of the budding yeast CCAN (also referred to as Ctf19 complex) (figure 4b) [144][145][146]. These structures contain CENP-…”

Section: The Inner Kinetochore: Ccan Structurementioning

confidence: 99%

“…Major recent progress has been made in understanding the structure of the budding yeast CCAN (also referred to as Ctf19 complex) ( figure 4 b ) [ 144 – 146 ]. These structures contain CENP-I Ctf3 , CENP-H Mcm16 , CENP-K Mcm22 , CENP-L Iml3 , CENP-N Chl4 , CENP-P Ctf19 , CENP-O Mcm21 , CENP-Q Okp1 , CENP-U Ame1 , CENP-T Cnn1 and CENP-W Wip1 , as well as Nkp1 and Nkp2, which apparently lack human homologues.…”

Section: The Inner Kinetochore: Ccan Structurementioning

confidence: 99%

“…A structure of the budding yeast Ctf3 complex (CENP-HIK) in the context of the CCAN/Ctf19 complex reveals the organization of this subcomplex ( figure 5 b ). The C-terminal region of CENP-I Ctf3 has multiple HEAT repeats, and a CENP-H Mcm16 -CENP-K Mcm22 coiled-coil motif fits into the concave surface of the CENP-I Ctf3 HEAT array [ 146 ]. The N-terminal region of CENP-I Ctf3 was separately shown to contain HEAT repeats just like the C-terminal region, and the interaction between the C-terminal region of CENP-I Ctf3 and CENP-H Mcm16 -CENP-K Mcm22 is mirrored at the other end of the complex [ 153 ].…”

Section: Cenp-hikmmentioning

confidence: 99%

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The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle

2020

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Eukaryotic chromosome segregation relies upon specific connections from DNA to the microtubule-based spindle that forms at cell division. The chromosomal locus that directs this process is the centromere, where a structure called the kinetochore forms upon entry into mitosis. Recent crystallography and single-particle electron microscopy have provided unprecedented high-resolution views of the molecular complexes involved in this process. The centromere is epigenetically specified by nucleosomes harbouring a histone H3 variant, CENP-A, and we review recent progress on how it differentiates centromeric chromatin from the rest of the chromosome, the biochemical pathway that mediates its assembly and how two non-histone components of the centromere specifically recognize CENP-A nucleosomes. The core centromeric nucleosome complex (CCNC) is required to recruit a 16-subunit complex termed the constitutive centromere associated network (CCAN), and we highlight recent structures reported of the budding yeast CCAN. Finally, the structures of multiple modular sub-complexes of the kinetochore have been solved at near-atomic resolution, providing insight into how connections are made to the CCAN on one end and to the spindle microtubules on the other. One can now build molecular models from the DNA through to the physical connections to microtubules.

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Section: The Inner Kinetochore: Ccan Structurementioning

confidence: 99%

Section: The Inner Kinetochore: Ccan Structurementioning

confidence: 99%

Section: Cenp-hikmmentioning

confidence: 99%

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The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle

2020

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“…As a sole HEAT protein and an essential subunit in kinetochore, the structure and function research of CENP‐I would be useful to understand kinetochore assembly and chromosome segregation. The recent Cryo‐EM structures had revealed the multiple interactions of CENP‐I and other subunits . However, the intramolecular interaction and structure details of CENP‐I itself have not been analyzed yet.…”

Section: Discussionmentioning

confidence: 99%

“…We previously reported the N‐terminal half structure of fungal CENP‐I that forms a ternary complex with C‐terminal heterodimer of fungal CENP‐H/K . The recent cryo‐EM structures revealed another half of Ctf3 (CENP‐I homolog), which forms complex with N‐terminal heterodimer of Mcm16/22 (CENP‐H/K homolog) . However, the intramolecular interaction and structure details of CENP‐I are less discussed.…”

Section: Introductionmentioning

confidence: 99%

Structural insights into the intramolecular interactions of centromere protein CENP‐I

Zhao

Cao

et al. 2020

J of Molecular Recognition

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In mitosis, the accurate segregation of sister chromosomes relies on kinetochore, a multiple subunits complex assembled on centromere of each sister chromosome. As a core component of inner kinetochore, CENP-I plays important functions to mediate kinetochore assembly and supports the faithful chromosome segregation. The structures of the N-terminus and C-terminus of CENP-I homologs in complex with CENP-H/K have been reported, respectively. Unfortunately, the intramolecular interactions of CENP-I are poorly understood, and how CENP-I interacts with CENP-M remains unknown. Here, we verified a unique helix α11, which forms the intramolecular interactions with N-terminal HEAT repeats in fungal CENP-I. Deletion of the helix α11 exposed the hydrophobic surface and resulted in the in vitro protein aggregation of N-terminal HEAT repeats of fungal CENP-I. The corresponding helix and its intramolecular interaction are highly conserved in human CENP-I. Deletion of the corresponding helix in human CENP-I dramatically reduced the functional activity to interact with CENP-H and CENP-M. Mutations of the conserved residues on the helix in human CENP-I significantly weakened the binding to CENP-M, but not CENP-H, in HeLa cells. Therefore, our findings for the first time unveiled a conserved helix of CENP-I, which is important for the intramolecular interaction and function, and would be helpful for understanding the structure basis of how CENP-I mediates the kinetochore assembly during cell cycle and mitosis. K E Y W O R D S centromere, computational protein structure, crystal structure, intramolecular interaction, kinetochore, protein-protein interaction

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Minichromosome maintenance proteins in eukaryotic chromosome segregation

et al. 2021

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Minichromosome maintenance (Mcm) proteins are well-known for their functions in DNA replication. However, their roles in chromosome segregation are yet to be reviewed in detail. Following the discovery in 1984, a group of Mcm proteins, known as the ARS-nonspecific group consisting of Mcm13, Mcm16-19, and Mcm21-22, were characterized as bonafide kinetochore proteins and were shown to play significant roles in the kinetochore assembly and high-fidelity chromosome segregation. This review focuses on the structure, function, and evolution of this group of Mcm proteins. Our in silico analysis of the physical interactors of these proteins reveals that they share non-overlapping functions despite being copurified in biochemically stable complexes. We have discussed the contrasting results reported in the literature and experimental strategies to address them. Taken together, this review focuses on the structure-function of the ARS-nonspecific Mcm proteins and their evolutionary flexibility to maintain genome stability in various organisms.

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The structure of the yeast Ctf3 complex

Cited by 19 publications

References 39 publications

The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle

The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle

Structural insights into the intramolecular interactions of centromere protein CENP‐I

Minichromosome maintenance proteins in eukaryotic chromosome segregation

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