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https://hdl.handle.net/2440/21896
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DC Field | Value | Language |
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dc.contributor.author | Reynolds, David M. | en |
dc.date.issued | 2002 | en |
dc.identifier.uri | http://hdl.handle.net/2440/21896 | - |
dc.description | "September, 2002." | en |
dc.description | Bibliography: leaves 93-106. | en |
dc.description | 106 leaves : ill. (some col.), plates ; 30 cm. | en |
dc.description.abstract | In this thesis the biochemical and genetic characterization of Fkh2p identifies it as a major component of SFF. It has been shown to bind DNA in an Mcm1p dependent manner and the Fkh2p DNA binding domain is essential for this interaction. The protein interaction domain of Mcm1p has been demonstrated to be essential for ternary complex formation. Fkh2p, along with a functionally redundant protein Fkh1p, has been show to control the periodic expression of the CLB2 cluster genes. The functional characterisation of the Fkh2p domains reveals an important role for both the Forkhead associated domain and the C-terminus. Ndd1p. another protein important for mitotic progression, is shown to be important for CLB2 cluster regulation by de-repressing Fkh2p and activating gene expression. The role of cdk activity is shown to act through the CLB2 cluster upstream activating sequences, possibly through Ndd1p. | en |
dc.format.extent | 132908 bytes | en |
dc.format.mimetype | application/pdf | en |
dc.language.iso | en | en |
dc.subject.lcsh | Saccharomyces cerevisiae Genetics. | en |
dc.subject.lcsh | Genetic transcription Regulation. | en |
dc.subject.lcsh | Cyclin-dependent kinases | en |
dc.title | Transcriptional regulation at the G2/M transition in the budding yeast, Saccharomyces cerevisiae / by David Matthew Reynolds. | en |
dc.type | Thesis | en |
dc.contributor.school | Dept. of Molecular Biosciences | en |
dc.provenance | This electronic version is made publicly available by the University of Adelaide in accordance with its open access policy for student theses. Copyright in this thesis remains with the author. This thesis may incorporate third party material which has been used by the author pursuant to Fair Dealing exception. If you are the author of this thesis and do not wish it to be made publicly available or If you are the owner of any included third party copyright material you wish to be removed from this electronic version, please complete the take down form located at: http://www.adelaide.edu.au/legals. | en |
dc.description.dissertation | Thesis (Ph.D.)--University of Adelaide, Dept. of Molecular Biosciences, 2003 | en |
Appears in Collections: | Research Theses |
Files in This Item:
File | Description | Size | Format | |
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01front.pdf | 129.79 kB | Adobe PDF | View/Open | |
02whole.pdf | 6.08 MB | Adobe PDF | View/Open |
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