Characterization of the Interaction Between MutL and the UvrD Helicase in the Methyl-directed DNA Mismatch Repair Pathway of E. Coli PDF Download
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Author: Steven Pattishall
Publisher:
ISBN:
Category :
Languages : en
Pages : 72
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Book Description
Author: Steven Pattishall
Publisher:
ISBN:
Category :
Languages : en
Pages : 72
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Book Description
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: Yerdos A. Ordabayev
Publisher:
ISBN:
Category : Electronic dissertations
Languages : en
Pages : 150
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E. coli UvrD is a superfamily 1A helicase/translocase involved in DNA repair, recombination, and replication. I investigated the role of E. coli MutL, a regulatory protein involved in methyl-directed mismatch DNA repair, in the regulation of UvrD-catalyzed DNA unwinding. Using single molecule fluorescence resonance energy transfer (FRET) and single round stopped-flow DNA unwinding experiments I demonstrated that MutL can activate latent UvrD monomer helicase activity and also stimulate UvrD dimer helicase activity. Furthermore, using analytical ultracentrifugation experiments I determined that a single MutL dimer is sufficient to activate UvrD monomer helicase. DNA unwinding experiments with a series of DNA substrates of varying duplex length under single round unwinding conditions showed that MutL increases the amount of duplex DNA unwound by UvrD in a single binding event. Therefore, MutL acts as a processivity factor by binding to and presumably moving along with UvrD during unwinding. I also showed that MutL requires contacts with the 3' ssDNA tail for optimal activation of UvrD helicase activity.The C-terminal tail of UvrD is highly variable among SF1A helicases and suggested to interact with MutL, however, the truncated UvrD[delta]73 mutant lacking its C-terminal tail is activated by MutL, indicating that the disordered C-terminal domain is not essential for stimulation. I also found that MutL is unable to activate the helicase activity of the structurally similar E. coli Rep helicase, indicating that MutL stimulation is specific to UvrD. Furthermore, MutL also fails to activate the helicase activity of chimeric UvrD containing the 2B sub-domain of Rep helicase. This result demonstrates that MutL activation of the monomeric UvrD helicase is regulated specifically by the 2B sub-domain of UvrD. Using single molecule and ensemble FRET experiments I showed that MutL binding to a UvrD monomer-DNA complex induces partial closing of the 2B sub-domain. Transient kinetic studies of MutL-induced activation of the UvrD helicase and MutL-induced changes in the UvrD 2B sub-domain showed that formation of the partially closed state is on the pathway to forming the active helicase. The kinetic analysis of these two sets of experiments revealed that under the experimentally used MutL concentrations the active MutL-UvrD species are formed predominantly through the conformational selection pathway (>90%) and to a lesser degree through the induced fit pathway (
Author:
Publisher: Academic Press
ISBN: 0123876664
Category : Science
Languages : en
Pages : 353
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Book Description
Written by research experts, this volume of Progress in Molecular Biology and Translational Science focuses on current science surrounding the mechanisms of DNA repair. - Contributions from leading authorities - Informs and updates on all the latest developments in the field
Author: Andrei Kuzminov
Publisher: Landes Bioscience
ISBN:
Category : Medical
Languages : en
Pages : 234
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Category : Cancer
Languages : en
Pages : 940
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Author: Robert D. Wells
Publisher: Springer
ISBN: 9781461415299
Category : Science
Languages : en
Pages : 0
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Molecular Life Sciences: An Encyclopedic Reference will focus on understanding biological phenomena at the level of molecules and their interactions that govern life processes. The work will include articles on genes and genomes, protein structure and function, systems biology using genomics and proteomics as the focus, molecular aspects of cell structure and function, unifying concepts and theories from biology, chemistry, mathematics and physics that are essential for understanding the molecular life sciences (including teaching perspectives and assessment tools), and basic aspects of the various experimental approaches that are used in the Molecular Life Sciences.
Author: Axel T. Brünger
Publisher: Yale University Press
ISBN: 9780300054026
Category : Science
Languages : en
Pages : 404
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Book Description
X-PLOR is a highly sophisticated computer program that provides an interface between theoretical foundations and experimental data in structural biology, with specific emphasis on X-ray crystallography and nuclear magnetic resonance spectroscopy in solution of large biological macro-molecules. This manual to X-PLOR Version 3.1 presents the theoretical background, syntax, and function of the program and also provides a comprehensive list of references and sample input files with comments. It is intended primarily for researchers and students in the fields of computational chemistry, structural biology, and computational molecular biology.
Author: Errol C. Friedberg
Publisher: American Society for Microbiology Press
ISBN: 1555813194
Category : Science
Languages : en
Pages : 2587
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Book Description
An essential resource for all scientists researching cellular responses to DNA damage. • Introduces important new material reflective of the major changes and developments that have occurred in the field over the last decade. • Discussed the field within a strong historical framework, and all aspects of biological responses to DNA damage are detailed. • Provides information on covering sources and consequences of DNA damage; correcting altered bases in DNA: DNA repair; DNA damage tolerance and mutagenesis; regulatory responses to DNA damage in eukaryotes; and disease states associated with defective biological responses to DNA damage.
Author: Juan-Luis Ramos
Publisher: Springer Science & Business Media
ISBN: 1441990860
Category : Science
Languages : en
Pages : 837
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Book Description
Pseudomonas comprises three volumes covering the biology of pseudomonads in a wide context, including the niches they inhabit, the taxonomic relations among members of this group, the molecular biology of gene expression in different niches and under different environmental conditions, the analysis of virulence traits in plants, animals and human pathogens as well as the determinants that make some strains useful for biotechnological applications and promotion of plant growth. There has been growing interest in pseudomonads and a particular urge to understand the biology underlying the complex metabolism of these ubiquitous microbes. These bacteria are capable of colonizing a wide range of niches, including the soil, the plant rhizosphere and phylosphere, and animal tissues; more recently they have attracted attention because of their capacity to form biofilms, a characteristic with potentially important medical and environmental implications. The three volumes cover the following topics: - Taxonomy, - Genomics, - Life styles, - Cell Architecture, - Virulence, - Regulation, - Macromolecules, - Alternative Respiratory Substrates, - Catabolism and Biotransformations. Pseudomonas will be of use to all researchers working on these bacteria, particularly those studying microbiology, plant crops, pathogenesis, and chemical engineering. Advanced students in biology, medicine and agronomy will also find these three volumes a valuable reference during their studies.
