- Abstract:
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Background: Cdc23/Mcm10 is required for the initiation and elongation steps of DNA replication but its biochemical function is unclear. Here, we probe its function using a novel approach in fission yeast, involving Cdc23 cleavage by the TEV protease. Results: Insertion of a TEV protease cleavage site into Cdc23 allows in vivo removal of the C-terminal 170 aa of the protein by TEV protease induction, resulting in an S phase arrest. This C-terminal fragment of Cdc23 is not retained in the nucle...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 2.6MB)
-
(pdf, 1.6MB)
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- Publisher copy:
- 10.1186/1471-2199-6-13
-
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- Publisher:
- Biomed Central Ltd. Publisher's website
- Journal:
- BMC Molecular Biology Journal website
- Volume:
- 6
- Pages:
- Article number 13
- Publication date:
- 2005-06-05
- DOI:
- ISSN:
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1471-2199
- URN:
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uuid:dcb273b3-9753-4f0b-b4be-7acd4809d477
- Local pid:
- ora:1687
- Language:
- English
- Subjects:
- Copyright holder:
- Yang et al.; licensee BioMed Central Ltd.
- Copyright date:
- 2005
- Notes:
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This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0),
which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Citation: Yang, X. et al. (2005). 'Nuclear distribution and chromatin association of DNA polymerase α-primase is affected by TEV protease cleavage of Cdc23 (Mcm10) in fission yeast', BMC Molecular Biology, 6: 13 (doi:10.1186/147-2199-6-13) [Available at http://www.biomedcentral.com/1471-2199/6/13].
Journal article
Nuclear distribution and chromatin association of DNA polymerase α-primase is affected by TEV protease cleavage of Cdc23 (Mcm10) in fission yeast
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Cancer Research UK
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