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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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.

Translational Regulation

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,...

Regulation of Expression at Multiple Steps

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the addition of a...

Regulation of Expression Occurs at Multiple Steps

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Regulation of Nuclear Protein Sorting

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Related Experiment Video

Updated: May 24, 2026

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

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

Published on: February 27, 2016

Regulation of sirtuin function by posttranslational modifications.

Franziska Flick¹, Bernhard Lüscher

¹Medical School, Institute of Biochemistry and Molecular Biology, RWTH Aachen University Aachen, Germany.

Frontiers in Pharmacology

|March 10, 2012

Summary

This summary is machine-generated.

Mammalian sirtuins, NAD(+)-dependent deacetylases, are crucial for cell survival and genome stability. Their N- and C-terminal extensions are key targets for posttranslational modifications, regulating sirtuin function and linking them to signaling pathways.

Keywords:

ADP-ribosylation NAD+-dependent deacetylation acetylation methylation phosphorylation proteolytic cleavage sumoylation

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Published on: February 27, 2020

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Last Updated: May 24, 2026

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

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

Published on: February 27, 2016

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Sirtuins (homologs of yeast Sir2) are NAD(+)-dependent enzymes with deacetylase, ADP-ribosyltransferase, demalonylase, and desuccinylase activities.
Mammalian sirtuins (SIRT1-7) share a catalytic core but have distinct N- and C-terminal extensions.
Sirtuins regulate vital cellular processes like survival, autophagy, apoptosis, DNA repair, and genome stability, and are linked to diseases such as cancer and neurodegeneration.

Purpose of the Study:

To review the posttranslational regulation mechanisms of mammalian sirtuins.
To discuss the relevance of these regulations in physiological processes.
To highlight the role of N- and C-terminal extensions in sirtuin function and signaling.

Main Methods:

Literature review of existing studies on sirtuin regulation.
Analysis of posttranslational modification (PTM) data for mammalian sirtuins.
Correlation of PTMs with sirtuin functions and associated signaling pathways.

Main Results:

Posttranslational modifications primarily target the N- and C-terminal extensions of sirtuins.
These modifications influence sirtuin function, potentially through interactions with the catalytic core domain.
Little is known about PTMs directly affecting the catalytic domain.

Conclusions:

The N- and C-terminal extensions play critical regulatory roles in controlling sirtuin functions.
PTMs of these extensions connect sirtuins to various cellular signaling pathways.
Further research is needed to elucidate PTMs of the catalytic domain and their regulatory impact.