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

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

6.9K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.9K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

6.0K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
6.0K
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

17.2K
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...
17.2K
Conserved Binding Sites01:49

Conserved Binding Sites

5.3K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.3K

You might also read

Related Articles

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

Sort by
Same author

Hiring a team: an integral selection procedure for inter- and transdisciplinary PhD candidates.

Humanities & social sciences communications·2026
Same author

Structure-function analysis of the bacterial ClpE-ClpP AAA+ protease.

The Journal of biological chemistry·2026
Same author

The bis-salphen Zn(II) unit: a versatile building block for self-assembled heteroleptic coordination cages.

Nanoscale·2026
Same author

The <i>Schizosaccharomyces pombe</i> Glycosyltransferase Gmh5 is a Functional Homologue of the α-1,6-Mannosyltransferase Mnn10 Crucial for N-Glycan Processing.

Food technology and biotechnology·2026
Same author

NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit.

Nature communications·2026
Same author

TRIM2 E3 ligase substrate discovery reveals zinc-mediated regulation of TMEM106B in the endolysosomal pathway.

EMBO reports·2026

Related Experiment Video

Updated: Mar 30, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

2.4K

Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.

Annemarie Horn1, Janosch Hennig2,3, Yasar L Ahmed1

  • 1Heidelberg University Biochemistry Center (BZH), INF 328, Heidelberg D-69120, Germany.

Nature Communications
|November 17, 2015
PubMed
Summary

Chloroplast light-harvesting protein delivery uses a soluble complex (cpSRP) that tethers to the Alb3 insertase via cpSRP43 chromodomain 3. This reveals a novel mechanism for membrane protein targeting.

More Related Videos

CRISPR-Mediated Reorganization of Chromatin Loop Structure
09:20

CRISPR-Mediated Reorganization of Chromatin Loop Structure

Published on: September 14, 2018

13.2K
Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

4.8K

Related Experiment Videos

Last Updated: Mar 30, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

2.4K
CRISPR-Mediated Reorganization of Chromatin Loop Structure
09:20

CRISPR-Mediated Reorganization of Chromatin Loop Structure

Published on: September 14, 2018

13.2K
Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

4.8K

Area of Science:

  • Chloroplast biology
  • Membrane protein biogenesis
  • Molecular mechanisms of protein targeting

Background:

  • Canonical membrane protein biogenesis relies on co-translational targeting via signal recognition particle (SRP).
  • Chloroplast light-harvesting chlorophyll a,b-binding proteins (LHCPs) are delivered post-translationally via a soluble complex (cpSRP).

Purpose of the Study:

  • To elucidate the molecular mechanisms of cpSRP tethering to the Alb3 insertase.
  • To understand the structural basis of ligand selectivity within cpSRP chromodomains.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • X-ray crystallography
  • Biochemical analyses

Main Results:

  • Identified a specific interaction between cpSRP43 chromodomain 3 and a linear motif in the Alb3 C-terminal tail for tethering.
  • Dissected the structural basis for selectivity of cpSRP chromodomains 2 and 3 for cpSRP54 and Alb3, respectively.
  • Explained negative cooperativity in ligand binding through dynamics in the chromodomain interface.

Conclusions:

  • Proposed a model for membrane recruitment of the cpSRP transit complex to Alb3.
  • Suggested that the tandem arrangement of chromodomains may confer functional advantages in protein targeting.