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Registration Number

0224U032893, (0124U004173) , R & D reports

Title

Highly homologous paralogs of translation elongation factor 1A. Structural studies to understand functional differences.

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Напрацювання препаративної кількості нативних білків eEF1A1 і eEF1A2.

Head

Negrutskii Borys S., д.б.н.

Registration Date

10-12-2024

Organization

Institute of Molecular Biology and Genetics of NAS of Ukraine

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The aim of the project is to define the structural organization of eEF1A1 and eEF1A2 in solution by creating their high-quality, experimentally validated structural models. We aim to precisely identify the structurally dynamic regions in both proteins, find out their differences, and show possible functional consequences of these differences for protein synthesis.

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 The goal of the scientific project is to elucidate the spatial organization of eEF1A1 and eEF1A2 in solution, accurately identify sites with varying structural dynamics, and uncover potential functional implications of differences in the spatial structures of these proteins. An additional influencing factor is the post-translational modifications of these proteins, particularly the methylation of lysine residues. Although the methylation sites have long been known, the functional role of this modification in translation factors remains unclear. Considering that methylated lysines are located on the protein surface, we hypothesize that this modification could potentially affect interactions with partner molecules, including other components of the protein synthesis system in cells. As a result of the project's first phase, the planned amounts of translation elongation factors eEF1A1 and eEF1A2 were obtained, sufficient for studying their structural organization using various physicochemical methods. Additionally, several mutants of the eEF1A1 protein were constructed, where methylated lysine residues were substituted with arginines, thus preventing further methylation of these sites. These mutants were shown to be expressible in human cells. The creation of such mutants is necessary for subsequent stages of the project, which will investigate the ability of mutant proteins to interact with partner proteins and their influence on protein synthesis in human cells.

Product Description

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Bondarchuk Tetiana V.
Novosylna Oleksandra V.
Porubleva Larysa V.
Shalak Viacheslav F.

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2024-12-10