H2020Индивидуална стипендия2015–2017

Protprot · Biophysical characterisation of a protein-activating protein-protein interaction

„Хоризонт 2020“ — Действия „Мария Склодовска-Кюри“

Период: 2015-08-01 → 2017-07-31
Финансиране от ЕС: 195 455 €
Участници: 1
Схема: MSCA-IF-EF-ST

Линиите свързват координатора с партньорите.

Накратко на български

Взаимодействието между два протеина (PPDK и PDRP), които регулират фотосинтезата при растения като царевицата, се анализира чрез биофизични методи. Познаването на тези механизми помага за подобряване на добивите при различни култури за храна.

Този кратък обзор е генериран от изкуствен интелект

Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.

Резултати накратко

Biophysical characterisation of a protein-activating protein-protein interaction

"Plants have found numerous strategies to adapt to a changing climate. On such strategy, C4 photosynthesis, is critical to how crop plants such as maize and sorghum can thrive in hot and dry climates. While we understand the chemistry of this adaptation, we do not understand the biochemistry and how precisely it is regulated and evolved. Deepening our klnowledge about the ""engines"" of C4 type photosynthesis is valuable for biotechnology and can have applications in improving the yields of other plants used as human food. In this project, we aimed to use biophysical approaches to understand the determinants of interaction between a protein central to the C4 pathway for photosynthetic CO2 fixation (PPDK) and the regulatory kinase with which it interacts. We wanted to elucidate the molecular mechanism of that unusual kinase that is dependent upon ADP rather than ATP. Our studies on that regulatory protein (PDRP) will also aid our understanding of other kinase enzymes. In particular, we aimed to use recently-described methodology for the incorporation of phosphoserine into proteins to generate per-phosphorylated proteins for model binding studies as well as chemical approaches developed in the host laboratory for the generation of model peptides containing analogues of phosphohistidine. That is because the interaction between PPDK and PDRP proteins is dependent upon the presence of a phosphothreonine residue in PPDK. It was shown that PPDK with phosphoserine in the place of phosphotreonine remains a substrate for PDRP. We also aimed to investigate the interaction of the regulatory protein with its small molecule ligands. "

Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз

Цел на проекта

Protein post-translational modification is an essential feature of living systems; one of the most common post-translational modifications is phosphorylation. Phosphorylation of proteins is central both to direct regulation of activity and to protein-protein interactions. Within this project we will use the study of a model regulatory protein-protein interaction, dependent upon phosphorylation to provide a training platform in biophysical and structural approaches to protein-protein interactions. The particular protein-protein interaction is the phosphohistidine/phosphothreonine-dependent interaction of the plant and bacterial enzyme, PPDK, with its regulatory protein PDRP. This regulatory protein appears to be central to the efficiency of photosynthesis in those plants using the C4 pathway of CO2 fixation as well as to the regulation of bacterial growth yet little is known about the molecular details of its action. Protein-protein interactions such as the PPDK-PDRP are ubiquitous in biological systems, it is the combination of thousands of such pair-wise interactions that lead to the collective properties of all cells. The ability to characterise each individual interaction thoroughly in vitro is essential for the continued development of both our understanding of the cell and how to manipulate this behaviour in therapeutics. Through this fellowship, the experienced researcher, Dr Witkowska, will gain essential hands-on experience with the application of the full range of contemporary approaches to such interactions which will enable her to establish herself as an independent researcher in the area upon her return to her home country while maintaining research links with the host laboratory.

Оригинален текст от CORDIS (на английски).

Участници

UNIVERSITY OF LEEDS · LeedsКоординаторОбединеното кралство