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TOC-maker SIGNED

The assembly and structure of the chloroplast protein import machinery in plants

Total Cost €

0

EC-Contrib. €

0

Partnership

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 TOC-maker project word cloud

Explore the words cloud of the TOC-maker project. It provides you a very rough idea of what is the project "TOC-maker" about.

analysing    respectively    predicted    complexes    stalled    cryo    experiments    homeostasis    difficult    de    plant    specialized    integration    composition    outer    purpose    equipped    techniques    tagged    purification    tic    sequence    majorly    transgenic    assembly    gap    photosynthetic    pulse    purified    cell    ribosomes    organization    electron    apparatus    toc    biogenesis    plants    biochemical    chloroplast    convert    compartment    reported    structural    multiprotein    solar    proper    chase    thaliana    proteins    configurations    elucidated    tightly    inner    interacting    machinery    mature    dynamic    abundant    microscopy    mechanisms    housekeeping    events    nucleus    assist    energy    enhanced    arabidopsis    transiently    polypeptides    encoded    protein    membranes    cells    expressing    components    epitope    photosynthesis    import    nascent    molecular    nature    enriched    affinity    synthesis    rapid    chloroplasts    etiolation    translocons    resolution    model    chemical    coupled    envelope    assembled   

Project "TOC-maker" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

Organization address
address: WELLINGTON SQUARE UNIVERSITY OFFICES
city: OXFORD
postcode: OX1 2JD
website: www.ox.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 224˙933 €
 EC max contribution 224˙933 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2019
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2020
 Duration (year-month-day) from 2020-06-01   to  2022-05-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD UK (OXFORD) coordinator 224˙933.00

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 Project objective

Plants convert solar energy into chemical energy by the process called photosynthesis in a specialized compartment of the cell known as chloroplasts. Chloroplasts are majorly enriched with nucleus-encoded proteins and to import them, chloroplast outer and inner envelope membranes are equipped with apparatus called the TOC and TIC translocons, respectively. For the TOC apparatus, there are two major configurations, TOC-P and TOC-H, reported so far, which import highly abundant, Photosynthetic and Housekeeping pre-proteins, respectively. TOC-P and TOC-H are multiprotein complexes which must be specifically assembled for proper development and homeostasis of the chloroplast. Due to the dynamic nature of the translocons, component synthesis and assembly must be rapid and tightly coupled, making the process difficult to investigate. Thus, understanding the mechanisms of the assembly process is both challenging and exciting. Biogenesis of TOC complexes is rapidly enhanced during chloroplast development or de-etiolation, and I will exploit this process to investigate the assembly of different TOC configurations, using the model plant Arabidopsis thaliana. For this purpose, transgenic plants expressing epitope-tagged TOC components and cells expressing nascent polypeptides of TOC components with stalled ribosomes will be generated. Proteins transiently interacting with new TOC components, which are predicted to assist integration and assembly of the TOC complex, will be studied by using affinity purification, pulse-chase experiments, and other biochemical techniques, and thus a sequence of assembly events will be elucidated. Although the molecular composition of the TOC protein import machinery has been well studied, the detailed structural organization of TOC complexes has not yet been elucidated. I will address this knowledge gap by analysing affinity-purified TOC complexes from mature chloroplasts at high resolution by cryo-electron microscopy.

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