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 Synthase: Structure01:18

ATP Synthase: Structure

18.1K
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...
18.1K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

19.2K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
19.2K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

5.2K
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...
5.2K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

6.9K
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...
6.9K
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

4.8K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
4.8K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

10.5K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
10.5K

You might also read

Related Articles

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

Sort by
Same author

Proceedings of the Canadian Society for Molecular Biosciences (CSMB) 2024 Conference - Gene Regulation: From Cells to Systems.

Biochemistry and cell biology = Biochimie et biologie cellulaire·2025
Same author

In silico based re-engineering of a computationally designed biosensor with altered signalling mode and improved dynamic range.

Archives of biochemistry and biophysics·2024
Same author

Differential roles of putative arginine fingers of AAA<sup>+</sup> ATPases Rvb1 and Rvb2.

bioRxiv : the preprint server for biology·2024
Same author

Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding.

Nature communications·2023
Same author

The prokaryotic activity of the IGR IRESs is mediated by ribosomal protein S1.

Nucleic acids research·2022
Same author

Introduction: Dual use in life science research.

Biochemistry and cell biology = Biochimie et biologie cellulaire·2022

Related Experiment Video

Updated: Apr 18, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
08:44

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

7.9K

The universally conserved NTPase OLA1.

Jessica Semmelrock1, Hans-Joachim Wieden2

  • 1Alberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, AB, Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|April 17, 2026
PubMed
Summary

The ancient translation factor OLA1, involved in diverse cellular processes and diseases, likely regulates protein synthesis through molecular mimicry with canonical factors. Understanding OLA1

Keywords:
GTPaseOLA1YchFmacromolecular mimicrytranslation factor

More Related Videos

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

19.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

3.0K

Related Experiment Videos

Last Updated: Apr 18, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
08:44

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

7.9K
Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

19.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

3.0K

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The non-canonical translation factor OBG-like ATPase 1 (OLA1) is evolutionarily conserved.
  • OLA1 has been linked to various cellular functions including metabolism, stress response, and disease.
  • Its diverse roles necessitate a deeper understanding of its molecular mechanism.

Purpose of the Study:

  • To elucidate the molecular mechanism of OLA1.
  • To explain the broad range of phenotypic traits associated with OLA1.
  • To investigate OLA1's role in translation regulation.

Main Methods:

  • Analysis of OLA1's protein structural domains.
  • In vivo studies of OLA1.
  • In vitro studies of OLA1.

Main Results:

  • Structural information suggests OLA1's involvement in translation.
  • In vivo and in vitro data support a role in ribosome-dependent processes.
  • Molecular mimicry with canonical translation factors is proposed.

Conclusions:

  • OLA1 likely functions as a regulator of ribosome-dependent translation.
  • Its mechanism may involve molecular mimicry.
  • Further research into OLA1's mechanism will clarify its diverse biological roles.