ArticleThe Journal of biological chemistry2012
Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Automated Fluorescence Lifetime Imaging High-Content Analysis of Förster Resonance Energy Transfer between Endogenously Labeled Kinetochore Proteins in Live Budding Yeast Cells.SLAS technology · 2019Article
- Architecture of the CBF3-centromere complex of the budding yeast kinetochore.Nature structural & molecular biology · 2018Article
- Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10.Cell reports · 2018Article
- Structural basis for assembly of the CBF3 kinetochore complex.The EMBO journal · 2018Article
- The unconventional kinetoplastid kinetochore: from discovery toward functional understanding.Biochemical Society transactions · 2016Review
- Review
- Utilization of protein intrinsic disorder knowledge in structural proteomics.Biochimica et biophysica acta · 2013Article
- Centromere Structure and Function.Progress in molecular and subcellular biologyReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have solved the x-ray structure of the N-terminal half of the yeast kinetochore protein Ndc10 at 1.9 Å resolution. This essential protein is a key constituent of the budding yeast centromere and is essential for the recruitment of the centromeric nucleosome and establishment of the kinetochore. The fold of the protein shows unexpected similarities to the tyrosine recombinase/λ-integrase family of proteins, most notably Cre, with some variation in the relative position of the subdomains. This finding offers new insights into kinetochore evolution and the adaptation of a well studied protein fold to a novel role. By comparison with tyrosine recombinases and mutagenesis studies, we have been able to define some of the key DNA-binding motifs.
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