ArticleNature2011
Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 135 citations in OpenAlex.
- Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026Review
- Remote homology and functional genetics unmask deeply preserved Scm3/HJURP orthologs in metazoans.Science advances · 2026Article
- Remote homology and functional genetics unmask deeply preserved Scm3/HJURP orthologs in metazoans.bioRxiv : the preprint server for biology · 2026Article
- Keeping it centered: decoding the activities that regulate yeast histone H3 variant Cse4 and confine it to centromeres.Frontiers in cell and developmental biology · 2026Review
- Epigenetic Regulatory Processes Involved in the Establishment and Maintenance of Skin Homeostasis-The Role of Microbiota.International journal of molecular sciences · 2025Review
- Non-nucleosomal (CENP-A/H4)bioRxiv : the preprint server for biology · 2025Article
- The Chaperone NASP Contributes to de Novo Deposition of the Centromeric Histone Variant CENH3 in Arabidopsis Early Embryogenesis.Plant & cell physiology · 2024Article
- Interaction of histone H4 with Cse4 facilitates conformational changes in Cse4 for its sumoylation and mislocalization.Nucleic acids research · 2024Article
- Uncovering natural allelic and structural variants of OsCENH3 gene by targeted resequencing and in silico mining in genus Oryza.Scientific reports · 2023Article
- Non-B-form DNA tends to form in centromeric regions and has undergone changes in polyploid oat subgenomes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Four Causes: The Functional Architecture of Centromeres and Kinetochores.Annual review of genetics · 2022Review
- Structural Mechanism of TAF-Iβ Chaperone Function on Linker Histone H1.10.Journal of molecular biology · 2022Article
- Cdc48Ufd1/Npl4 segregase removes mislocalized centromeric histone H3 variant CENP-A from non-centromeric chromatin.Nucleic acids research · 2022Article
- Simple-to-use CRISPR-SpCas9/SaCas9/AsCas12a vector series for genome editing in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2021Article
- Kinetochore assembly throughout the cell cycle.Seminars in cell & developmental biology · 2021Article
- Reduced gene dosage of histone H4 prevents CENP-A mislocalization and chromosomal instability in Saccharomyces cerevisiae.Genetics · 2021Article
- Structural and dynamic mechanisms of CBF3-guided centromeric nucleosome formation.Nature communications · 2021Article
- CENP-A nucleosome-a chromatin-embedded pedestal for the centromere: lessons learned from structural biology.Essays in biochemistry · 2020Review
- Article
- Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex.Life science alliance · 2019Article
25 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
The centromere is a unique chromosomal locus that ensures accurate segregation of chromosomes during cell division by directing the assembly of a multiprotein complex, the kinetochore. The centromere is marked by a conserved variant of conventional histone H3 termed CenH3 or CENP-A (ref. 2). A conserved motif of CenH3, the CATD, defined by loop 1 and helix 2 of the histone fold, is necessary and sufficient for specifying centromere functions of CenH3 (refs 3, 4). The structural basis of this specification is of particular interest. Yeast Scm3 and human HJURP are conserved non-histone proteins that interact physically with the (CenH3-H4)(2) heterotetramer and are required for the deposition of CenH3 at centromeres in vivo. Here we have elucidated the structural basis for recognition of budding yeast (Saccharomyces cerevisiae) CenH3 (called Cse4) by Scm3. We solved the structure of the Cse4-binding domain (CBD) of Scm3 in complex with Cse4 and H4 in a single chain model. An α-helix and an irregular loop at the conserved amino terminus and a shorter α-helix at the carboxy terminus of Scm3(CBD) wraps around the Cse4-H4 dimer. Four Cse4-specific residues in the N-terminal region of helix 2 are sufficient for specific recognition by conserved and functionally important residues in the N-terminal helix of Scm3 through formation of a hydrophobic cluster. Scm3(CBD) induces major conformational changes and sterically occludes DNA-binding sites in the structure of Cse4 and H4. These findings have implications for the assembly and architecture of the centromeric nucleosome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.