Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
ABC Transporters: Exporter01:31

ABC Transporters: Exporter

ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Seizure worsening and sodium channel blockers in HCN1-related epilepsies: A case series.

Developmental medicine and child neurology·2026
Same author

Infection cycles of viruses of the phylum Nucleocytoviricota.

Nature reviews. Microbiology·2026
Same author

TRIP8b<sub>nano</sub> peptide prevents cAMP binding to HCN2 channels alleviating pain-like behaviors in rats with neuropathic pain.

The Journal of physiology·2026
Same author

Combining elastic network models and linear response theory as tool to understand the global dynamics in allosteric regulation of HCN channels.

The Journal of general physiology·2026
Same author

Comprehensive classification of HCN1 variants linked to neurodevelopmental disorders with and without epilepsy.

bioRxiv : the preprint server for biology·2026
Same author

AMPK-mediated HCN4 channel phosphorylation contributes to age-related intrinsic bradycardia.

The Journal of general physiology·2026

Related Experiment Video

Updated: Jun 12, 2026

Live Calcium Imaging of Virus-Infected Human Intestinal Organoid Monolayers Using Genetically Encoded Calcium Indicators
08:01

Live Calcium Imaging of Virus-Infected Human Intestinal Organoid Monolayers Using Genetically Encoded Calcium Indicators

Published on: January 19, 2024

A functional calcium-transporting ATPase encoded by chlorella viruses.

Maria Cristina Bonza1, Holger Martin, Ming Kang

  • 1Dipartimento di Biologia e Istituto di Biofisica del CNR, Università degli Studi di Milano, Milano, Italy.

The Journal of General Virology
|June 25, 2010
PubMed
Summary

This study identifies and characterizes viral calcium pumps (Ca(2+) pumps) from chlorella viruses. These viral pumps transport both calcium and manganese ions, exhibiting unique properties distinct from cellular counterparts.

More Related Videos

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

Forward Genetic Screen Using Transgenic Calcium Reporter Aequorin to Identify Novel Targets in Calcium Signaling
08:46

Forward Genetic Screen Using Transgenic Calcium Reporter Aequorin to Identify Novel Targets in Calcium Signaling

Published on: August 1, 2020

Related Experiment Videos

Last Updated: Jun 12, 2026

Live Calcium Imaging of Virus-Infected Human Intestinal Organoid Monolayers Using Genetically Encoded Calcium Indicators
08:01

Live Calcium Imaging of Virus-Infected Human Intestinal Organoid Monolayers Using Genetically Encoded Calcium Indicators

Published on: January 19, 2024

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

Published on: September 28, 2018

Forward Genetic Screen Using Transgenic Calcium Reporter Aequorin to Identify Novel Targets in Calcium Signaling
08:46

Forward Genetic Screen Using Transgenic Calcium Reporter Aequorin to Identify Novel Targets in Calcium Signaling

Published on: August 1, 2020

Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • Calcium-transporting ATPases (Ca(2+) pumps) are essential for cellular calcium homeostasis.
  • These pumps are found across all cellular organisms, maintaining critical ion gradients.
  • Viral genes encoding functional proteins are increasingly recognized for their roles in host-pathogen interactions.

Purpose of the Study:

  • To identify and functionally characterize calcium pumps encoded by chlorella viruses.
  • To investigate the phylogenetic placement and unique properties of viral Ca(2+) pumps.
  • To determine if viral Ca(2+) pumps possess distinct substrate specificities or regulatory mechanisms.

Main Methods:

  • Sequence and phylogenetic analyses of viral genes.
  • Complementation assays using a triple yeast mutant (K616).
  • In vitro ATPase activity assays and vanadate inhibition studies.
  • Analysis of phosphorylated intermediate formation.

Main Results:

  • Two putative Ca(2+) pumps, M535L and C785L, were identified in chlorella viruses MT325 and AR158.
  • M535L demonstrated Ca(2+) and, unusually, manganese ion transport activity.
  • Viral Ca(2+) pumps belong to group IIB of P-type ATPases but lack a calmodulin-binding domain.
  • ATPase activity was basal, vanadate-inhibited, and not significantly stimulated by Ca(2+) or Mn(2+).
  • A vanadate-sensitive phosphorylated intermediate was observed, confirming unique enzymatic properties.

Conclusions:

  • This is the first report of a functional P-type Ca(2+)-transporting ATPase encoded by a virus.
  • Viral Ca(2+) pumps exhibit distinct characteristics compared to their cellular homologs, including dual ion transport (Ca(2+)/Mn(2+)).
  • The findings provide insights into viral strategies for manipulating host cell ion concentrations and potential novel therapeutic targets.