Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596318
Title: Structural studies of transcriptional regulators
Author: Ball, L. J.
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 1997
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Abstract:
Both of the proteins studied in this work are involved in the control of gene expression at the transcriptional level. The first project described in this thesis involves the elucidation of the precise zinc co-ordination in the native zinc form of the PPR1 DNA-binding domain. PPR1 is a transcriptional activator found in the yeast, Saccharomyces cerevisiae, which specifically binds DNA in order to activate a series of genes involved in pyrimidine biosynthesis. The zinc-binding domain of PPR1 is highly conserved across a large number of yeast transcriptional activators and is important for the recognition of the palindromic CGG-(N)n-CCG DNA sequence to which these proteins bind (where n is the number of nucleotides (N) which separate the CGG triplets). EXAFS spectroscopy revealed that each zinc atom in the cluster was co-ordinated by four cysteinyl sulphur atoms in a two-metal ion cluster. The sulphur ligands were at distances of 2.28 A and 2.41 A from the zinc, indicating terminal and bridging sulphurs, respectively, and the directly measured Zn-Zn separation was 3.16 A. Preliminary nuclear magnetic resonance (NMR) spectroscopic studies were also carried out on the same fragment in the hope that the structure of the PPR1 linker and dimerization domains, responsible for sequence specificity, could also be elucidated from these studies, but the NMR spectra were not of sufficient quality to allow a structure determination. The second project concentrates on the structure determination of the N-terminal domain of the mouse modifier protein, MoMOD1, which contains a highly conserved region known as the 'chromo' domain. The chromo domains are thought to be indirectly involved in modification of chromatin structure, by directing other proteins to particular sites on chromatin.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.596318  DOI: Not available
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