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DC Field | Value | Language |
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dc.contributor.advisor | Gupta, Radhey | - |
dc.contributor.author | Hassan, F M Nazmul | - |
dc.date.accessioned | 2018-04-23T16:41:54Z | - |
dc.date.available | 2018-04-23T16:41:54Z | - |
dc.date.issued | 2017-12 | - |
dc.identifier.uri | http://hdl.handle.net/11375/22740 | - |
dc.description.abstract | The Deinococcus species are highly resistant to oxidation, desiccation, and radiation. Very few characteristics explain these unique features of Deinococcus species. This study reports the results of detailed comparative genomics, structural and protein-protein interactions studies on the DNA repair proteins from Deinococcus species. Comparative genomics studies have identified a large number of conserved signature indels (CSIs) in the DNA repair proteins that are specific for Deinococcus species. In parallel, I have carried out the structural and protein-protein interactions studies of CSIs which are present in nucleotide excision repair (NER), UV damage endonuclease (UvsE)-dependent excision repair (UVER) and homologous recombination (HR) pathways proteins. Comparative genomics studies have identified a 30 amino acid (aa) conserved signature indel (CSI) in the UvrA1 protein and a 1 aa CSI in the UvsE protein that are specific for Deinococcus species. I also have identified a 1 aa CSI in the RecA protein that is specific for Deinococcus-Thermus phylum. Structural analysis delineates that these CSIs are located at the surface loop of the protein. Protein-protein interactions analyses reveal that the UvsE protein of Deinococcus species is present in a genetic linkage with Zn-ribbon protein. RecA protein is also present in a genetic linkage with two proteins in Deinococcus-Thermus phylum. UvsE and RecA proteins are predicted to be part of same operon with the interacting proteins. The UvrA protein is also present in genetic linkage with disulfide oxidoreductase (DsbA), disulfide bond formation protein (DsbB) and one of our labs identified conserved signature protein (CSP). These four proteins are indicated to be part of the same operon. We have proposed a model to understand the functional role of these four proteins in together in DNA repair. According to our model, the predicted linkage of the UvrA protein via CSP to the DsbA/DsbB is expected to restore the activity of the NER pathway in Deinococcus species upon radiation exposure. Further experimental studies may lead to prove our hypothesis and to understand the functional role of CSI and CSP among Deinococcus species. Similarly, I have carried out the comparative genomics studies in the GyrA and GyrB protein sequences which are supposed to play role in regulation of temporal gene expression during intracellular development. I have identified a number of molecular markers in the form of CSIs in the GyrA and GyrB protein sequences which are specific for all the members of Chlamydiae. Structural analysis indicates that two of these CSIs may play role in enhancing the supercoiling activity of GyrA and GyrB proteins of chlamydial species. I have carried out protein-protein interactions analyses to understand the functional role of other two CSIs of GyrA and GyrB proteins. Protein-protein interactions analyses delineate that the GyrA and GyrB proteins of chlamydial species are present in a unique genetic linkage with thymidylate kinase (TMK), DNA polymerase III subunit δ' (HolB) and one of the chlamydial specific CSP. We have proposed a model to understand the functional role of CSIs, CSP and also to delineate the functional role of these proteins together to chlamydial intracellular development. According to our model, these five proteins together play a role to increase the replication rate during the midcycle of intracellular development. CSP and CSIs are responsible for these unique associations among these proteins. Further experimental studies may lead to prove this hypothesis and will guide to decipher the intricateness of chlamydial intracellular development. | en_US |
dc.language.iso | en | en_US |
dc.title | Functional Significance of novel molecular markers specific for Deinococcus and Chlamydiae species | en_US |
dc.type | Thesis | en_US |
dc.contributor.department | Biochemistry and Biomedical Sciences | en_US |
dc.description.degreetype | Thesis | en_US |
dc.description.degree | Master of Health Sciences (MSc) | en_US |
Appears in Collections: | Open Access Dissertations and Theses |
Files in This Item:
File | Description | Size | Format | |
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Hassan_F M Nazmul_December2017_MSc.pdf | 6.22 MB | Adobe PDF | View/Open |
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