Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

Insertion of Multi-pass Transmembrane Proteins in the RER

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

Intralumenal Vesicles and Multivesicular Bodies

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

You might also read

Related Articles

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

Sort by

Same author

Environmental Impact of β-Cyclodextrin Complexes with Herbicides: A Study on Solubility and Toxicity.

Molecules (Basel, Switzerland)·2026

Same author

Correction: The protein corona at the nano-bio interface: the need for standardized methodology and opportunities for neurodegenerative disease intervention.

RSC advances·2026

Same author

Identification and Optimization of a Truncated Hs-1-Derived Antimicrobial Peptide for Enhanced Broad-Spectrum Antiviral Activity.

ChemMedChem·2026

Same author

The protein corona at the nano-bio interface: the need for standardized methodology and opportunities for neurodegenerative disease intervention.

RSC advances·2026

Same author

Structural and Dynamics Insights into Melatonin Binding to MT1 Receptor.

Chembiochem : a European journal of chemical biology·2026

Same author

Special Issue "Application of NMR Spectroscopy in Biomolecules".

International journal of molecular sciences·2026

Search research articles

Related Experiment Video

Updated: Jun 27, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Identifying Two New Ros/MucR Proteins: An Atypical Structure with a Divergent Function.

Domenico Sgambati¹, Ilaria Imperatrice¹, Enza Canonico¹

¹Department of Environmental, Biological, Pharmaceutical Sciences and Technologies, University of Campania "Luigi Vanvitelli", Via Vivaldi 43, 81100 Caserta, Italy.

|June 26, 2026

Summary

Two new Ros/MucR proteins in Sinorhizobium meliloti, MucR2 and MucR3, were identified. They exhibit unique structural and DNA-binding properties, suggesting diverse gene regulation mechanisms within the Ros/MucR family.

Keywords:

H-NS-like proteins Ros/MucR family protein–DNA interaction

More Related Videos

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

Published on: October 3, 2017

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Related Experiment Videos

Last Updated: Jun 27, 2026

An Integrated Approach for Microprotein Identification and Sequence Analysis

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging

Published on: October 3, 2017

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Area of Science:

Bacterial genetics and molecular biology
Protein structure and function
Microbial pathogenesis

Background:

The Ros/MucR family comprises proteins regulating genes essential for host interactions.
These proteins are classified as H-NS-like in α-proteobacteria, influencing gene expression and genome structure.
Understanding Ros/MucR function is key to deciphering bacterial adaptation and pathogenicity.

Purpose of the Study:

To identify and characterize novel Ros/MucR family members in Sinorhizobium meliloti.
To investigate the structural and functional differences of these new MucR proteins compared to known homologs.
To elucidate their DNA-binding and oligomerization capabilities.

Main Methods:

Cryogenic electron microscopy (cryo-EM) for structural analysis.
Mass spectrometry and light scattering for oligomerization studies.
Nuclear magnetic resonance (NMR) and electrophoretic mobility shift assay (EMSA) for DNA interactions.
Biochemical assays to assess DNA bridging activity.

Main Results:

Identification of two new Ros/MucR members, MucR2 and MucR3, in Sinorhizobium meliloti.
MucR2 lacks the typical circular oligomeric structure, while MucR3 exhibits concentration-dependent oligomerization with low circularity.
Both MucR2 and MucR3 bind DNA but lack the DNA bridging activity essential for genome structuring.
A novel zinc coordination sphere was identified in MucR2 and MucR3.

Conclusions:

The Ros/MucR family employs distinct mechanisms for gene expression control.
MucR2 and MucR3 represent novel variants with unique structural and functional properties.
These findings provide a foundation for studying the cooperative roles of multiple MucR proteins in bacterial gene regulation.