Mechanisms of DNA Repair.
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| Imprint: | Elsevier Science & Technology 2012. |
|---|---|
| Description: | 1 online resource (353 pages) |
| Language: | English |
| Series: | Progress in Molecular Biology and Translational Science Ser. Vol. 110 Progress in Molecular Biology and Translational Science Ser. ; Vol. 110. |
| Subject: | |
| Format: | E-Resource Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/12378394 |
Table of Contents:
- Front Cover; Mechanisms of DNA Repair; Copyright; Contents; Contributors; Preface; Chpater 1: Dynamics of Lesion Processing by Bacterial Nucleotide Excision Repair Proteins; I. Structural Insights of Bacterial Nucleotide Excision Repair; A. Overview of the Process; B. Dynamics of the UvrA2B2-DNA Complex; C. Kinetic Proofreading as Part of a Dynamic DNA Damage Recognition Process: Role of ATP; II. So Few DNA Repair Proteins, So Much DNA: Defining the Big Problem; A. Challenge of Repair Inside a Bacterial Cell; B. Potential Modes of Damage Site Location
- C. Necessary Experimental Components to Observe Single Molecules in ActionIII. Damage Searching by UvrA2 and UvrA2B2; IV. Future Directions; A. Observing Protein Nanomachines at Work; B. Overcoming the Brownian Motion Barrier; References; Chpater 2: Transcription-Coupled DNA Repair in Prokaryotes; I. Introduction; II. Background: Genomic Heterogeneity in NER and the Discovery of TCR; III. The Role of RNA Polymerase in TCR; IV. The Role of Mfd in TCR; V. The Role of UvrA in TCR; VI. The Role of UvrB in TCR; VII. Other Examples of Transcription-Related DNA Damage Processing in Bacteria; A. NusA
- B. Base Excision RepairVIII. Conclusions; Acknowledgments; References; Chpater 3: The Functions of MutL in Mismatch Repair: The Power of Multitasking; I. Overview of DNA Mismatch Repair; A. DNA Mismatch Repair in Escherichia coli; B. Strand Discrimination in Mismatch Repair in Organisms Lacking MutH; C. The Multiple Faces of MutL; II. MutL is a Multidomain Protein; A. The ATPase Domain; B. DNA Binding; C. The Dimerization Domain; III. Architecture of the Endonuclease Domain; A. The Endonuclease Site; B. MutL is an Mn2+-Dependent Endonuclease; C. The Regulatory Zn2+-Binding Site
- D. The Endonuclease Activity of MutLIV. Regulation of the Endonuclease Activity of MutL; A. DNA Binding; B. Stimulatory Effect of the Processivity Clamp; C. Mismatch Dependency; V. Concluding Remarks; References; Chpater 4: The Fpg/Nei Family of DNA Glycosylases: Substrates, Structures, and Search for Damage; I. Introduction; II. Fpg/Nei Phylogeny; III. Fpg/Nei Structures; A. Introduction; B. Substrate Preference; C. Comparison of Structures of the Fpg/Nei Family; IV. Glycosylases Search for Lesions; V. Concluding Remarks; Acknowledgments; References
- Chpater 5: Regulation of Base Excision Repair in Eukaryotes by Dynamic Localization StrategiesI. Base Excision Repair; A. Requirements and Limitations of Base Excision Repair; B. Regulation of BER: Current Concepts and Observations; C. Dynamic Localization; II. Dynamic Localization of BER Proteins; A. General Pathway; B. Requirements to Dynamically Localize; C. Examples of Dynamic Localization in Response to Genotoxic Stress; D. Insight into Dynamic Localization; III. Hypotheses on the Orchestration of Dynamic Localization; References