Interaction of the E. Coli Single-stranded DNA-binding Protein with Nucleic Acids and Its Comparison with Protamine PDF Download
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Author: Shirin W. Hasan
Publisher:
ISBN:
Category : Carboxypeptidases
Languages : en
Pages : 158
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Book Description
Author: Shirin W. Hasan
Publisher:
ISBN:
Category : Carboxypeptidases
Languages : en
Pages : 158
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 77
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Book Description
Author: Frederick W. Perrino
Publisher:
ISBN:
Category : DNA.
Languages : en
Pages : 366
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Book Description
Author: Thomas A. Steitz
Publisher: CUP Archive
ISBN: 9780521414890
Category : Science
Languages : en
Pages : 108
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Book Description
In this 1993 text, Nobel Prize winner Professor Steitz reviews the wide-ranging research in structural studies of DNA-binding proteins and their complexes with DNA. The author clearly and concisely describes the uses of techniques in molecular genetics, DNA synthesis, protein crystallography and nuclear magnetic response.
Author: Duo Lu
Publisher:
ISBN:
Category :
Languages : en
Pages : 149
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 71
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Book Description
Author: Leslie Bruce Overman
Publisher:
ISBN:
Category : DNA repair
Languages : en
Pages : 362
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Book Description
Author: Donald E. Johnson
Publisher:
ISBN:
Category :
Languages : en
Pages : 242
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Book Description
Author: Jane M. Weisemann
Publisher:
ISBN:
Category : Amino acids
Languages : en
Pages : 140
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Book Description
The DNA replication machinery (replisome) is a dynamic multi-protein complex that efficiently achieves the task of genome duplication. However, DNA replication is a vulnerable process to organisms due to the generation of single-stranded (ss) DNA intermediates. In addition, the DNA replication fork must overcome obstacles, such as template damage or frozen protein complexes, that threaten accurate and complete genome duplication. Cells encode specialized ssDNA-binding proteins (SSBs) to bind ssDNA and ensure the genomic template is maintained. The Escherichia coli (E. coli) SSB has also been found to interact with over a dozen proteins involved in the major genome maintenance pathways. The RNase HI enzyme specifically hydrolyzes the RNA in RNA:DNA hybrids and is involved in processing DNA replication lagging strand RNA primers as well as removing transcription-dependent R-loops that block replication fork progression. In this work I have confirmed and characterized the interaction between E. coli RNase HI and SSB. The protein complex is maintained through SSB's highly conserved C-terminal tail (SSB-Ct). I located the SSB-Ct docking site on RNase HI and identified the binding pocket residues that are essential for maintaining the interaction in vitro. The RNase HI/SSB interaction stimulates RNase HI-mediated RNA:DNA hybrid hydrolysis by lowering the reaction's Km, suggesting that SSB recruits RNase HI to its substrate. I have tested this hypothesis in cells by incorporating an SSB binding mutant identified from in vitro experiments, rnhAK60E, into the chromosome. The SSB interaction mediates the localization of RNase HI to the DNA replication fork but does not impact the role of RNase HI in lagging strand RNA primer processing. However, combining the point mutant with a Rep (accessory helicase localized to the replication fork) null mutant (rnhAK60E rep) renders cells sensitive to rich media and increases DNA damage. The rnhAK60E rep phenotype is influenced by mutations in RNA Polymerase likely arising from changes to levels of transcription-dependent R-loops. From the data presented in this thesis we have generated a model for the function of the RNase HI/SSB complex that provides a mechanism for localizing the cellular activity of the RNase HI enzyme.
