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

Long-patch Base Excision Repair01:02

Long-patch Base Excision Repair

7.7K
Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
7.7K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.4K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

10.4K
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...
10.4K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.2K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.2K
GTPases and their Regulation02:14

GTPases and their Regulation

9.6K
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
9.6K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

6.2K
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
6.2K

You might also read

Related Articles

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

Sort by
Same author

Workshop report: Clinical training and integration of genetic counselors into interprofessional teams in the German-speaking countries.

Genetics in medicine open·2024
Same author

A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein.

Nature communications·2024
Same author

Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly.

Proceedings of the National Academy of Sciences of the United States of America·2022
Same author

Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.

Nature communications·2021
Same author

Regulation of DEAH-box RNA helicases by G-patch proteins.

Biological chemistry·2021
Same author

Dimer Organization of Membrane-Associated NS5A of Hepatitis C Virus as Determined by Highly Sensitive <sup>1</sup> H-Detected Solid-State NMR.

Angewandte Chemie (International ed. in English)·2020

Related Experiment Video

Updated: Dec 26, 2025

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
07:15

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation

Published on: November 26, 2011

18.1K

Structural basis for DEAH-helicase activation by G-patch proteins.

Michael K Studer1, Lazar Ivanović1, Marco E Weber1

  • 1Institute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH) Zürich, 8093 Zürich, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|March 18, 2020
PubMed
Summary

The G-patch motif acts as a flexible brace, enhancing RNA helicase DHX15 activity by tethering its core to C-terminal domains. This structural insight reveals how G-patch activators boost essential RNA processing functions.

Keywords:
DEAH/RHA helicaseG-patch proteinsribosome biogenesissplicing

More Related Videos

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
10:59

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair

Published on: May 24, 2017

10.0K
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
11:25

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

9.9K

Related Experiment Videos

Last Updated: Dec 26, 2025

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
07:15

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation

Published on: November 26, 2011

18.1K
Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
10:59

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair

Published on: May 24, 2017

10.0K
A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
11:25

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

9.9K

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • DEAH/RHA RNA helicases are crucial for RNA metabolism, including splicing and ribosome biogenesis.
  • These helicases remodel RNA-protein complexes by coupling ATP hydrolysis to conformational changes.
  • G-patch activators significantly enhance DEAH helicase activity, but the mechanism remains unclear.

Purpose of the Study:

  • To elucidate the molecular basis of G-patch-mediated activation of DEAH helicases.
  • To determine the structure of human helicase DHX15 in complex with the NKRF G-patch motif.

Main Methods:

  • X-ray crystallography was used to solve the structure of DHX15 bound to the NKRF G-patch.
  • Structural analysis was performed in the presence and absence of adenosine diphosphate (ADP).
  • Mutagenesis studies were conducted to assess the impact of G-patch binding on helicase function.

Main Results:

  • The G-patch motif binds DHX15 in an extended conformation, tethering the catalytic core to C-terminal domains.
  • This binding fixes a conformation favorable for RNA binding and enhances RNA affinity, helicase, and ATPase activity.
  • Mutations disrupting the G-patch tethering significantly reduce activation, indicating the importance of the brace-like function.

Conclusions:

  • The G-patch motif acts as a flexible brace, restricting excessive domain motions while maintaining catalytic flexibility.
  • This mechanism explains how G-patch activators enhance DHX15's RNA binding and catalytic efficiency.
  • The findings provide crucial molecular insights into the regulation of DEAH helicases in RNA metabolism.