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

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

12.9K
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...
12.9K
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

5.7K
Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
5.7K
The Proteasome Structure01:17

The Proteasome Structure

2.2K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
2.2K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.2K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
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...
2.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

1.0K
1.0K

You might also read

Related Articles

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

Sort by
Same author

Structural basis for transcriptional regulation by the cell division regulator MraZ in Mycoplasma genitalium.

Nature communications·2026
Same author

Mass spectrometry footprinting reveals how kinetic stabilizers counteract transthyretin dynamics altered by pathogenic mutations.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

A Fluorometric Assay to Compare SUMO Isoform Preferences in the SENP/ULP Family.

Methods in molecular biology (Clifton, N.J.)·2025
Same author

The SOX11:SMARCA4 complex is a driver of oncogenic transcriptional programs in mantle cell lymphoma.

Blood cancer journal·2025
Same author

Analysis of Protein Inhibitors of Trypsin in Quinoa, Amaranth and Lupine Seeds. Selection and Deep Structure-Function Characterization of the <i>Amaranthus caudatus</i> Species.

International journal of molecular sciences·2025
Same author

ChIP-seq and structural analyses delineating the regulatory mechanism of master regulator EsrB in <i>Edwardsiella piscicida</i>.

Applied and environmental microbiology·2024

Related Experiment Video

Updated: May 4, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

8.8K

Structural insights into the SENP6 Loop1 structure in complex with SUMO2.

Kamela O Alegre1, David Reverter

  • 1Institut de Biotecnologia i de Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.

Protein Science : a Publication of the Protein Society
|January 16, 2014
PubMed
Summary

SENP proteases cleave SUMO from proteins. Researchers engineered a SENP2 protease with a unique Loop1 insertion, revealing novel structural interactions and enhanced activity on diSUMO2 and polySUMO2 substrates.

Keywords:
SENP2SENP6SENP7SUMOpolySUMO chainubiquitin-like protein

More Related Videos

Quantitative FRET F&#246;rster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination
16:02

Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination

Published on: February 21, 2013

18.0K
In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
09:40

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

6.6K

Related Experiment Videos

Last Updated: May 4, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

8.8K
Quantitative FRET F&#246;rster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination
16:02

Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination

Published on: February 21, 2013

18.0K
In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
09:40

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

6.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • SENP proteases regulate SUMOylation by cleaving SUMO from target proteins.
  • SENP6 and SENP7 possess unique insertions in their catalytic domains, influencing their activity and specificity.
  • The Loop1 insertion is critical for SUMO2/3 activity and specificity in SENP6 and SENP7.

Purpose of the Study:

  • To investigate the structural role of the Loop1 insertion in SENP proteases.
  • To gain insights into the unique interface formed by SENP6/7 with SUMO2.
  • To understand how Loop1 influences the proteolytic activity of SENP proteases.

Main Methods:

  • Designed a chimeric SENP2 protease incorporating the Loop1 insertion from SENP6/7.
  • Determined the crystal structure of the SENP2-Loop1 chimera in complex with SUMO2 at 2.15 Å resolution.
  • Performed functional assays using SUMO substrates to assess proteolytic activity.

Main Results:

  • The crystal structure revealed an interface exclusive to SENP6/7 and unique contacts between SENP2-Loop1 and SUMO2.
  • The SENP2-Loop1 chimera exhibited increased proteolytic activity towards diSUMO2 and polySUMO2 substrates.
  • Structural data provided detailed insights into the molecular basis of SENP6/7 specificity.

Conclusions:

  • The Loop1 insertion is a key determinant of SENP6/7 activity and specificity.
  • The engineered SENP2-Loop1 chimera serves as a valuable tool for studying SENP protease function.
  • Understanding these structural and functional aspects can inform research on SUMOylation regulation.