- Title
- A comparative bioinformatic analysis of zinc binuclear cluster proteins
- Creator
- Mthombeni, Jabulani S
- Subject
- Bioinformatics
- Subject
- Zinc proteins
- Subject
- GABA
- Date Issued
- 2005
- Date
- 2005
- Type
- Thesis
- Type
- Masters
- Type
- MSc
- Identifier
- vital:4004
- Identifier
- http://hdl.handle.net/10962/d1004064
- Identifier
- Bioinformatics
- Identifier
- Zinc proteins
- Identifier
- GABA
- Description
- Members of the zinc binuclear cluster family are important fungal transcriptional regulators sharing a common DNA binding domain. Da181p is a pleotropic zinc binuclear cluster protein involved in the induction of the UGA genes required for the γ-aminobutyrate nitrogen catabolic pathway in Saccharomyces cerevisiae. The zinc binuclear cluster domain is indispensable for function in Da181p and little is known about other domains in this protein. The aim of the study was to explore the zinc binuclear cluster protein family using comparative bioinformatics as a complement to biochemical and structural approaches. A database of all zinc binuclear cluster proteins was composed. A total of 118 zinc binuclear proteins are reported in this work. Thirty nine previously unidentified zinc binuclear cluster proteins were found. Four homologues of Da181p were identified by homology searching. Important sequence motifs were identified in the aligned sequences of Da181p and its homologues. The coiled coil motif found in the Ga14p zinc binuclear cluster protein could not be identified in Da181p and its homologues. This suggested that Da181p did not dimerise through this structural motif as other zinc binuclear cluster proteins. Solvent accessible site that could be phosphorylated by protein kinase C or casein kinase II and the role of such sites in the possible regulation of Da181p function were discussed.
- Format
- 86 p.
- Format
- Publisher
- Rhodes University
- Publisher
- Faculty of Science, Biochemistry, Microbiology and Biotechnology
- Language
- English
- Rights
- Mthombeni, Jabulani S
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RU Department of Biochemistry, Microbiology and Biotechnology (end of 2014)
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