The structural characterization of two proteins involved in the repair of general DNA damage
Başlık çevirisi mevcut değil.
- Tez No: 403392
- Danışmanlar: Dr. TRACEY BARRETT
- Tez Türü: Doktora
- Konular: Genetik, Radyoloji ve Nükleer Tıp, Genetics, Radiology and Nuclear Medicine
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 2007
- Dil: İngilizce
- Üniversite: University of London - Birkbeck
- Enstitü: Yurtdışı Enstitü
- Ana Bilim Dalı: Belirtilmemiş.
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: 196
Özet
Özet yok.
Özet (Çeviri)
Several modes of repair exist to correct altered/damaged or mispaired bases in DNA. In this thesis the main focus will be on two Nucleotide excision repair (NER) mechanisms that recognise lesions associated with UV damage. In bacteria, the main mechanism for the removal of such adducts is the UvrABC pathway, pivotal to which is the damage recognition element UvrB that forms part of a tracking complex with UvrA. The dynamics underlying this process and in particular, the transformation of UvrB into an active helicase that is key to the location of lesions, were poorly understood. In order to gain insights into this essential step of the UvrABC pathway, the crystal structure of a ternary complex involving UvrB from B. subtilis bound to both ADP and a thymine trinucleotide was determined. This structure has not only shown that UvrB cycles between DNA binding competent and incompetent states but demonstrates that these changes are intrinsically linked to ATP hydrolysis. In addition to mainstream NER, a limited number of organisms possess an alternative mechanism that is initiated by a single, broad specificity damage specific endonuclease, UVDE. The way in which damage was detected by this unique family of enzymes could only be speculated based on the available data. The crystal structures of two UVDE-DNA complexes were determined revealing elements essential for lesion recognition and processing. These include the identification of a non-specific nucleotide binding pocket shown to be key to DNA binding.
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