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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

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Updated: May 7, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

The E1 proteins.

Monika Bergvall1, Thomas Melendy, Jacques Archambault

  • 1Molecular Virology Laboratory, Institut de recherches cliniques de Montréal (IRCM), 110 Pine avenue West, Montreal, QC, Canada H2W 1R7; Department of Microbiology and Immunology, McGill University, Montreal, QC, Canada.

Virology
|September 14, 2013
PubMed
Summary
This summary is machine-generated.

Papillomavirus E1 helicase (E1) is crucial for viral DNA replication. This review details E1

Keywords:
ATPaseDNA replicationE1EpisomeHelicasePapillomavirusPhosphoryaltionPost-translational modifications

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Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Papillomaviruses (PVs) encode a single essential enzyme, the E1 ATP-dependent DNA helicase.
  • E1 orchestrates viral episome replication and amplification within infected cell nuclei.
  • E1 interacts with host DNA replication machinery to facilitate viral genome maintenance.

Purpose of the Study:

  • To review the functional domains of the papillomavirus E1 helicase.
  • To emphasize E1's interactions with DNA, host replication factors, and modifying enzymes.
  • To provide insights into how PVs utilize host cell machinery for replication.

Main Methods:

  • Review of biochemical and structural studies on E1.
  • Analysis of E1 assembly, DNA unwinding mechanisms (spiral escalator), and regulation.
  • Examination of post-translational modifications impacting E1 nuclear accumulation.

Main Results:

  • E1 assembles into a double-hexamer at the viral origin of replication.
  • E1 unwinds DNA at the origin and ahead of the replication fork.
  • Post-translational modifications tightly regulate E1 activity and nuclear localization.

Conclusions:

  • E1 is a well-characterized helicase providing insights into viral DNA replication strategies.
  • Understanding E1's interactions reveals how PVs exploit host cell processes.
  • E1's regulation is key to controlling viral genome amplification.