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Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Translational Regulation01:29

Translational Regulation

Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

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.
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Related Experiment Video

Updated: May 13, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Sirt1 activation by resveratrol is substrate sequence-selective.

Mahadevan Lakshminarasimhan1, David Rauh, Mike Schutkowski

  • 1Department of Biochemistry, University of Bayreuth, Bayreuth, Germany.

Aging
|March 26, 2013
PubMed
Summary

Resveratrol

Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Drug Discovery

Background:

  • Sirtuins, particularly Sirtuin 1 (SIRT1), are critical protein deacetylases and significant therapeutic targets.
  • The efficacy of pharmacological SIRT1 activation is debated, as the in vitro activator resveratrol shows inconsistent effects on physiological substrates.

Purpose of the Study:

  • To investigate the impact of substrate sequence on resveratrol's modulation of SIRT1 activity.
  • To identify specific acetylation sites and their sequence features influenced by resveratrol.

Main Methods:

  • Utilized peptide microarrays to analyze resveratrol's effects on SIRT1-dependent deacetylation across 6802 physiological acetylation sites.
  • Employed solution assays and statistical analysis to confirm and characterize substrate categories based on sequence features.

More Related Videos

A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae
10:39

A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae

Published on: September 17, 2020

Related Experiment Videos

Last Updated: May 13, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae
10:39

A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae

Published on: September 17, 2020

Main Results:

  • Resveratrol differentially modulated SIRT1 activity, stimulating deacetylation at a subset of sites and inhibiting it at others.
  • Most tested acetylation sites were minimally affected by resveratrol, highlighting substrate-specific responses.
  • Statistical analysis identified distinct sequence features correlating with resveratrol's stimulatory or inhibitory effects.

Conclusions:

  • SIRT1 modulation by resveratrol is highly dependent on the substrate's amino acid sequence.
  • These findings provide insights into the mechanism of resveratrol action and suggest specific substrates involved in its observed effects.
  • The study underscores the importance of substrate specificity in understanding and developing sirtuin-targeting therapeutics.