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Translation

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life

Translation

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life

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.

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

Pleiotropy

Pleiotropy

Pleiotropy is the phenomenon in which a single gene impacts multiple, seemingly unrelated phenotypic traits. For example, defects in the SOX10 gene cause Waardenburg Syndrome Type 4, or WS4, which can cause defects in pigmentation, hearing impairments, and an absence of intestinal contractions necessary for elimination. This diversity of phenotypes results from the expression pattern of SOX10 in early embryonic and fetal development. SOX10 is found in neural crest cells that form melanocytes,...

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Related Experiment Video

Updated: Jun 24, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Sumoylation and human disease pathogenesis.

Kevin D Sarge¹, Ok-Kyong Park-Sarge

¹Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536, USA. kdsarge@uky.edu

Trends in Biochemical Sciences

|March 14, 2009

Summary

Protein sumoylation regulates protein function and is linked to diseases like cancer and neurodegenerative disorders. New findings show sumoylation of amyloid precursor protein and lamin A may impact Alzheimer's disease and dilated cardiomyopathy.

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

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

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

Published on: November 2, 2017

Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Sumoylation, a post-translational modification, is crucial for protein function.
Dysregulation of sumoylation is implicated in various human diseases, including neurodegenerative conditions and cancer.
Specific disease-associated proteins are increasingly identified as SUMO-modified targets.

Purpose of the Study:

To identify novel disease-associated proteins that undergo SUMO modification.
To investigate the role of sumoylation in the pathogenesis of Alzheimer's disease and familial dilated cardiomyopathy.

Main Methods:

Proteomic analysis to identify SUMO-modified proteins.
Biochemical assays to confirm sumoylation.
Cellular and molecular biology techniques to assess protein function and disease relevance.

Main Results:

Amyloid precursor protein (APP) and lamin A were identified as novel SUMO-modified proteins.
Sumoylation of APP influences amyloid-beta peptide levels, suggesting a role in Alzheimer's disease.
Decreased sumoylation of lamin A was associated with familial dilated cardiomyopathy.

Conclusions:

Sumoylation plays a significant role in modulating the function of disease-associated proteins.
Targeting sumoylation pathways may offer therapeutic strategies for Alzheimer's disease and dilated cardiomyopathy.
This study expands the understanding of sumoylation's involvement in human pathology.