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TOPICAL COLLECTIONS

Current Research Methods to Analyze the Process of Protein Synthesis and Translational Output

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Ulrike Topf

Ulrike Topf

Polish Academy of Sciences

Dr. Ulrike Topf is an assistant professor and research group leader at the Institute of Biochemistry and Biophysics of the Polish Academy of Sciences in Warsaw. Her research interests comprise the identification of molecular mechanisms necessary to restore protein homeostasis upon cellular stress conditions and aging utilizing yeast and nematodes as model organisms. Particularly, Dr. Topf is analysing how the protein synthesis machinery in the cytosol adapts to accommodate the demands of the cell for newly synthesized proteins under oxidative stress conditions. Her latest research suggests that oxidative modifications of ribosomal proteins might provide a means of modulating translation. Dr. Topf performed her doctoral studies in the Friedrich Miescher Institute for Biomedical Research (FMI) in Switzerland and completed her postdoctoral training in the International Institute of Molecular and Cell Biology in Warsaw (IIMCB) and at the University of Warsaw. Currently, Dr. Topf is expanding her research program to investigate the role of protein folding mechanisms downstream of protein synthesis to overcome cellular stress conditions that lead to translation attenuation.         

Collection Overview

Protein synthesis (translation) is a fundamental cellular process governed by multifaceted machinery. During translation the information encoded in the messenger RNA is transformed into polypeptide chains. The process of translation is extensively studied and proceeds through three main phases: initiation, elongation and termination. Because the synthesis of proteins is vital for all cellular functions the process is very well controlled and can be adjusted to the needs of the cell.

Besides protein folding and degradation, the production of proteins is an essential process that protein homeostasis relies on. Many exogenous and endogenous stresses can influence the process of translation and consequently, the translational output. Nowadays, research challenges in protein translation involve the identification of the molecular mechanisms that facilitate the adaptation of protein synthesis. In this context, the ribosome itself became a major interest in the field. The ribosome was thought of to be a macromolecular complex consisting of proteins and RNA with little regulatory capacity. Over the past few years the concept of ‘specialized ribosomes’ developed. Such specialization occurs through heterogeneity in ribosomal protein composition and post-translational modifications, ribosomal RNA diversity, and differential binding of ribosome associated proteins. Thus, ribosome specialization may have an important influence on the production of functional proteins from the genomic template.       

This Methods Collection will gather approaches on assessing the process of protein synthesis, the rate of translation, the analysis of ribosomes including their purification and composition, and the identification of translational output.          

Articles

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

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Cited by 1

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2021

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Abstracts

RIBO-seq in bacteria: quick and easy sample collection and library preparation protocol for NGS sequencing

Olga Chrobak1,

Natalia Kopik1,

Agata Starosta*1,

Mariia Kovalenko1,

Przemysław Latoch2

1Laboratory of Gene Expression, ECOTECH-Complex, Maria Curie-Sklodowska University, ul. Gleboka 39, 20-612 Lublin, Poland; Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Sklodowska University, ul. Akademicka 19, 20-400 Lublin, Poland,

2Laboratory of Gene Expression, ECOTECH-Complex, Maria Curie-Sklodowska University, ul. Gleboka 39, 20-612 Lublin, Poland; Faculty of Information Technology, Polish-Japanese Academy of Information Technology, ul. Koszykowa 86, 02-008 Warsaw, Poland

FRET Assay for Characterizing Dynamic Protein Exchange Between Protein Assemblies

Reid Gordon*1

1University of California, Santa Barbara