Nuclear import of Cdc13 limits chromosomal capping
| Autor: | Raymund J. Wellinger, Erin Bonnell, Sofiane Y Mersaoui |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Telomere Capping Telomere-Binding Proteins Active Transport Cell Nucleus Context (language use) Saccharomyces cerevisiae Karyopherins Genome Integrity Repair and Replication Biology 03 medical and health sciences Genetics medicine Amino Acid Sequence Karyopherin Cell Nucleus chemistry.chemical_classification Binding Sites Sequence Homology Amino Acid fungi DNA Telomere 3. Good health Cell biology Cell nucleus 030104 developmental biology medicine.anatomical_structure chemistry Cytoplasm Mutation Protein Multimerization Nuclear transport Nuclear localization sequence Protein Binding |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | Cdc13 is an essential protein involved in telomere maintenance and chromosome capping. Individual domain analyses on Cdc13 suggest the presence of four distinct OB-fold domains and one recruitment domain. However, it remained unclear how these sub-domains function in the context of the whole protein in vivo. Here, we use individual single domain deletions to address their roles in telomere capping. We find that the OB2 domain contains a nuclear localization signal that is essential for nuclear import of Cdc13 and therefore is required for chromosome capping. The karyopherin Msn5 is important for nuclear localization, and retention of Cdc13 in the nucleus also requires its binding to telomeres. Moreover, Cdc13 homodimerization occurs even if the protein is not bound to DNA and is in the cytoplasm. Hence, Cdc13 abundance in the nucleus and, in consequence, its capping function is strongly affected by nucleo-cytoplasmic transport as well as nuclear retention by DNA binding. |
| Databáze: | OpenAIRE |
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