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Related Concept Videos

The Replisome03:01

The Replisome

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DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
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Translesion DNA Polymerases02:10

Translesion DNA Polymerases

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
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Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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DNA Helicases00:55

DNA Helicases

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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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Proofreading01:31

Proofreading

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Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase...
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Updated: May 25, 2025

Functional Imaging of Viral Transcription Factories Using 3D Fluorescence Microscopy
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DNA-Binding Activities of KSHV DNA Polymerase Processivity Factor (PF-8) Complexes.

Jennifer Kneas Travis1,2, Megan Martin1, Lindsey M Costantini1

  • 1Department of Biological and Biomedical Sciences, North Carolina Central University, Durham, NC 27707, USA.

Viruses
|February 26, 2025
PubMed
Summary

Researchers explored Kaposi's Sarcoma Herpesvirus (KSHV) processivity factor (PF-8) to find new antiviral targets. Understanding PF-8's DNA binding and ring formation is key to disrupting KSHV replication.

Keywords:
HHV-8KSHVelectron microscopyhuman herpesvirusesviral replication

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Quantitative Fluorescence In Situ Hybridization FISH and Immunofluorescence IF of Specific Gene Products in KSHV-Infected Cells
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Quantitative Fluorescence In Situ Hybridization FISH and Immunofluorescence IF of Specific Gene Products in KSHV-Infected Cells
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Quantitative Fluorescence In Situ Hybridization FISH and Immunofluorescence IF of Specific Gene Products in KSHV-Infected Cells

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Kaposi's Sarcoma Herpesvirus (KSHV) causes significant human diseases, with limited treatment options.
  • KSHV oncogenesis and infection spread rely on its lytic cycle, including genome replication.
  • The KSHV processivity factor (PF-8) is crucial for viral DNA replication and a potential antiviral target.

Purpose of the Study:

  • To characterize the Kaposi's Sarcoma Herpesvirus (KSHV) processivity factor (PF-8) at the single-molecule level.
  • To elucidate the molecular interactions of PF-8 involved in initiating viral DNA replication.
  • To identify PF-8's role in KSHV genome replication for potential antiviral strategies.

Main Methods:

  • Single-molecule characterization of PF-8 using transmission electron microscopy.
  • DNA positional mapping to determine PF-8 binding sites within the lytic origin of replication (OriLyt).
  • Multi-variable analysis of PF-8 DNA-binding activity with mutant OriLyts.

Main Results:

  • PF-8 forms oligomeric ring structures (tetramer, hexamer, dodecamer), similar to Epstein-Barr virus BMRF1.
  • High-frequency binding of PF-8 was observed at the KSHV lytic origin of replication (OriLyt).
  • Analysis revealed insights into how PF-8 associates with DNA and forms multi-ring structures.

Conclusions:

  • The study enhances mechanistic understanding of PF-8's protein-DNA and protein-protein interactions.
  • Characterization of PF-8 provides a foundation for developing novel KSHV antiviral therapies.
  • Targeting PF-8's role in DNA replication could disrupt the KSHV infectious cycle.