Quantitative Analysis and the Identification of Proteins that Interact with the Single-stranded DNA-binding Protein of Escherichia Coli PDF Download
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Author: Frederick W. Perrino
Publisher:
ISBN:
Category : DNA.
Languages : en
Pages : 366
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Author: Frederick W. Perrino
Publisher:
ISBN:
Category : DNA.
Languages : en
Pages : 366
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Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 77
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Author: Shirin W. Hasan
Publisher:
ISBN:
Category : Carboxypeptidases
Languages : en
Pages : 158
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Category :
Languages : en
Pages : 71
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Author: Duo Lu
Publisher:
ISBN:
Category :
Languages : en
Pages : 149
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Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 264
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In bacterial cells, most if not all replication forks encounter some form of DNA damage or roadblock that stall or inactivate the fork during normal cell growth. Numerous pathways exist for repairing and reactivating replication forks and these pathways are crucial for maintaining genome stability and cell viability. Bacterial "Maintenance of Genome Stability Protein A" (MgsA) and related eukaryotic enzymes are implicated in cellular responses to stalled DNA replication processes. MgsA enzymes are members of the clamp loader clade of AAA+ proteins but their structures and biochemical properties are poorly characterized. We describe the first complete crystal structure of Escherichia coli MgsA that reveals a highly intertwined homotetrameric arrangement for the protein that distinguishes it from other clamp-loader clade AAA+ proteins. An extended oligomerization domain relative to the clamp loader proteins accounts for the unique oligomeric state. The structure represents the inactive conformation of MgsA due to displacement of the arginine finger residues from the neighboring active sites. Thus, a conformational rearrangement is required to engage the arginine finger and activate MgsA ATPase activity. Association with double stranded DNA ends appears to be the trigger that induces the conformational rearrangement and activates ATP hydrolysis. We also describe a potential switch residue, Arginine92, that appears to coordinate DNA binding and ATP hydrolysis within MgsA. MgsA physically interacts with the single-stranded DNA binding protein (SSB). The interaction requires SSB's highly conserved C terminus (SSB Ct) and we define a likely SSB Ct binding site on MgsA. This interaction adds another member to the growing list of SSB interacting proteins and we propose that the interaction is critical for proper MgsA localization to the replisome. Collectively, this thesis presents a structural and biochemical characterization of Escherichia coli MgsA and provides insights into the mechanisms of MgsA-family proteins.
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Category :
Languages : en
Pages :
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Exonuclease I (ExoI) from Escherichia coli is a monomeric enzyme that processively degrades single stranded DNA in the 3' to 5' direction and has been implicated in DNA recombination and repair. It functions in numerous genome maintenance pathways, with particularly well defined roles in methyl-directed mismatch repair (MMR). The Escherichia coli MMR pathway can be reconstituted in vitro with the activities of eight proteins (8). MutS, MutL and MutH are involved in initiation of repair including mismatch recognition and generation of a nick at a nearby GATC sequence (53, 54, 55, 56). The hemimethylated state of GATC sequences immediately following replication serves as a signal to direct repair to the nascent strand of the DNA duplex (57, 58). DNA helicase II and one of several exonucleases (Exonucleas I, Exonuclease VII and RecJ) are required to excise the error-containing DNA strand beginning at the nicked GATC site (34, 35). Restoration of the correct DNA sequence by repair synthesis involves DNA polymerase III holoenzyme and SSB, and the final nick is sealed by DNA ligase (34). To identify interactions with ExoI involved in MMR repair system, we used the yeast two-hybrid system with ExoI as bait. By screening an E.coli genomic library, E. coli DNA helicase II (UvrD) was identified as a potential interacting protein. UvrD has been shown to be required for DNA excision repair, methyl-directed mismatch repair and has some undefined, role in DNA replication and recombination. In this report, in vitro experiments confirm that UvrD and ExoI make a direct physical interaction that may be required for function of the methyl-directed mismatch repair. Werner Syndrome is a rare autosomal recessive disease characterized by a premature aging phenotype, genomic instability and a dramatically increased incidence of cancer and heart disease. Mutations in a single gene encoding a 1,432 amino-acid helicase/exonuclease (hWRN) have been shown to be responsible for the development o
Author: Lakshmi N. Chilukuri
Publisher:
ISBN:
Category : Bacterial proteins
Languages : en
Pages : 314
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Author: Wayne P. Olson
Publisher: CRC Press
ISBN: 9780935184822
Category : Medical
Languages : en
Pages : 418
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This book focuses on practical, proven applications to automate the microbial identification process economically and with greater levels of safety and quality for patients. A diverse group of recognized experts survey the topic and present the latest techniques and technologies for microbial detection. They cover bacteria and yeasts, the technology of automation, equipment, methods, and the validation issues involved in "going automated." They also explore the challenges of detection and quantititation of contaminants in the increasing number of biologic injectable drugs and identify current trends in the industry. Features
Author: Leslie Bruce Overman
Publisher:
ISBN:
Category : DNA repair
Languages : en
Pages : 362
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