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What is the goal of DNA replication
Our general long-term goal is to determine the detailed molecular mechanisms by which the proteins and nucleic acids involved in the central dogma of molecular biology (DNA replication, transcription, and translation) achieve their biological functions. Virtually all aspects of the maintenance and expression of information stored in the genome involve interactions between proteins and nucleic acids. Over the past three decades we have obtained detailed structural insights into the mechanisms by which specific proteins and nucleic acids catalyze and control the fundamental processes of DNA replication, mRNA synthesis, and protein synthesis, as well as DNA recombination.
We have also determined the structures of another B-family DNA polymerase, phi29 DNA polymerase, which initiates replication by attaching the first nucleotide of the phage genome to a serine side chain of protein primer called terminal protein, as well as its binary and ternary substrate complexes. The basis of DNA strand displacement activity exhibited by this enzyme is explained by the template strand passing through a tunnel that is too small to accommodate the nontemplate strand that is displaced. The extreme processivity of this polymerase is explained by its topological encirclement of the substrate and product DNA at the active site. The structure of the phi29 DNA polymerase bound to terminal protein provides the first structural insights into the mechanism of protein-primed DNA replication, suggesting that a four-helix domain containing the priming serine must back out of the duplex DNA product-binding site as DNA synthesis proceeds.
with the processes of DNA replication and protein synthesis
The main goal of our team is understanding the mechanisms that stabilize replication forks facing natural barriers to their progression (such as highly transcribed genes) and are mediated by specialized molecular machines as DNA topoisomerases and helicases. We also focus in understanding how cells coordinate stalled replication fork signalling, through the DNA damage checkpoint response, with the mechanisms in charge of maintaining their integrity for DNA synthesis and that process them to prevent the accumulation of chromosome abnormalities.
DNA replication is the fascinating process allowing living organisms to grow and propagate by rapidly generating virtually identical copies of their genetic material. However, replication has a dark side for the cell as it is carried out in specialized structures (i.e. replication forks) that are intrinsically fragile and prone to engage in unscheduled recombination events. Replication fork progression is hampered when DNA synthesis is inhibited or when forks interfere with other chromosome metabolic processes (e.g. gene transcription or DNA repair). In situations replication forks tend to collapse and generate DNA breaks. Aberrant repair of collapsed forks, particularly in the context of a defective cellular response to DNA damage, give rise to mutations and chromosomal rearrangements, hallmarks of malignant transformation.
processes of DNA replication, mRNA synthesis, ..
It initially identifies how information essential for life is stored in DNA and then explains the processes of DNA replication, Mitosis and Meiosis....
The topic is the donation of my DNA for a research study; the goal of the study will be to find a variant of a gene that will resist specific bacterial diseases.
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DNA Replication & Protein Synthesis - Videos & …
Wilkins and Rosalind Franklin used X-ray diffraction to study DNA through its images, and it was on April 1953 that they finally published the discovery of the structure of DNA; they discovered how the hereditary information is coded on the DNA as well as its replication.
This interesting chapter presents the concept of DNA replication, ..
According to Alcamo (1996), each strand of the DNA double helix can act as a template for the synthesis of a new complementary strand as it contains a sequence of nucleotides that is exactly complementary to the nucleotide sequence of its p...
its about DNAreplication and Protein Synthesis!? | …
DNA methylation is a postreplicative modification that occurs when a methyl (-CH3) group is added at position 5 of the cytosine pyrimidine ring and “establishes a silent chromatin state by collaborating with proteins that modify nucleosomes.” (Rudolf Jaenisch, 2003)....
the fundamental processes of DNA replication, mRNA synthesis, ..
To establish the structural basis of DNA replication, we have been studying DNA polymerases and associated proteins involved in replication. Following on our earlier structures of Escherichia coli DNA polymerase I Klenow fragment and Thermus aquaticus DNA polymerase and their DNA substrate complexes, we established the crystal structure of a replicative DNA polymerase (from phage RB69) that is homologous to the eukaryotic B-family polymerases. The structures of the RB69 polymerase complexed with duplex DNA substrate, bound both at the editing site and the polymerase site, and of the sliding clamp complexed with a polymerase carboxyl-terminal peptide allowed construction of a replisome core structure. These structures showed that this macromolecular machine, charged with the responsibility of faithfully copying the DNA genome, undergoes large conformational changes throughout its catalytic cycle. These changes are associated with the enzyme's fidelity-enhancing mechanisms and translocation.
Unit 5: DNA Replication and Protein Synthesis - …
Toward our goal of understanding eubacterial replication, we determined the structure of the T. aquaticus DNA polymerase III, which we discovered exhibits no similarity to that of the archaeal or eukaryotic replicating polymerases, but rather possesses a catalytic domain that is homologous to that of repair DNA polymerase. Furthermore, our structure of a ternary complex of Pol III with substrates shows that the DNA and nucleoside triphosphate (NTP) substrates bind identically in these two polymerases. The possibility that the last common ancestor had a ribozyme-replicating polymerase is thus raised. Our structures of the hexomeric DnaB helicase and its complex with the helicase-binding domain of primase are beginning to illuminate the structural bases of primosome function.
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