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12 months Engineer Assistant position available at I2BC

Institute for Integrative Biology of the Cell (I2BC) CNRS UMR9198

Background

Chloroplasts (Cp) evolved from engulfed prokaryotes, most likely cyanobacteria that once lived as independent organisms. Thus, for many aspects chloroplasts are much more similar to bacteria. Nonetheless, the new cellular resident quickly evolved acquiring original and unique features as the lost or relocation of the majority of the genes to the nucleus of the host while only about 80- protein encoding genes remained in the organelle.

All nuclear and plastid-encoded chloroplast-localized proteins undergo many co- and post-translational modifications (CTMs and PTMs). This implies that both types of modifications may provide a substantial control for stability, accumulation, activity, assembly, and compartmentalisation. However, CTMs and PTMs of plastid proteins and their catalytic modifiers have not intensively been explored up to date. This particularly holds true for N-terminal Protein Modifications (NPMs).

The earliest NPM is the essential N-terminal methionine excision (NME). NME corresponds to the removal of the first amino acid incorporated in any nascent peptide chain (iMet). In plastids, MetAPs, the specific modifiers responsible for iMet excision, ensure NME. Still, a number of exceptions to the established NME rules exist in plastid, suggesting that pMetAPs might function differently from previously characterized MetAPs. Of note, the most unusual, intricate maturation mechanism of the N-ter of one of the subunits (RbcL) of the enzyme RuBisCO, which is the major component of the Calvin-Benson cycle ans the most abundant protein on earth, is a conundrum for decades as well as is its implication on RubisCO activity, assembly, localization or interaction with partners.

 

Project

The goal of this one-year project is the elucidation of the unique plastid machinery involved in RbcL processing. For this project we are looking for an Engineer Assistant with strong expertise in molecular biology, protein biochemistry and enzymology. Experience in mass spectrometry targeted techniques, enrichment of post-translational modification will be appreciated. The selected person will be in charge of the biochemical characterization of NPM modifiers and analysis of the impact of NPMs on RuBiscCO in E. coli.  The hired person will be trained to use our in-house pipelines/methods for the proteomics N-terminal characterization and quantification, NAT and MetAP enzymatic evaluation and partners sample analyses by MS. The successful candidate should be able to perform autonomously the experiments, analyze and interpret the emerging data. The ideal candidate is expected to be highly motivated and capable to have a strong relational and organizational sense. Fluency in English is preferred.

For further information please contact: Carmela GIGLIONE: carmela.giglione@i2bc.paris-saclay.fr

Carmela Giglione PhD

Protein Maturation, Cell fate and Therapeutics

Institute for Integrative Biology of the Cell (I2BC)

CNRS UMR9198, Bâtiment 21, 1 avenue de la Terrasse
F-91198 Gif-sur-Yvette cedex, France
E-mail: carmela.giglione@i2bc.paris-saclay.fr
Tel: 01 69 82 46 44
http://www.i2bc.paris-saclay.fr/spip.php?article130

 

To apply it is required:

  • A CV
  • Full Contact details of at least two references

 

Selected Publications of the group:

Castrec B, et al (2018) Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern. Nat Chem Biol 14: June 11, DOI: 10.1038/s41589-018-0077-5

Majeran W, et al (2018) Targeted profiling of A. thaliana sub-proteomes illuminates new co- and post-translationally N-terminal Myristoylated proteins. Plant Cell 30: 543–562

Bienvenut WV, Giglione C, Meinnel T (2015) Proteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state and upon deformylation inhibition. Proteomics 15: 2503-18

Bienvenut WV, Giglione C, Meinnel T (2017) SILProNAQ: A Convenient Approach for Proteome-Wide Analysis of Protein N-Termini and N-Terminal Acetylation Quantitation. Methods Mol Biol 1574: 17-34

Bienvenut WV, et al (2017) EnCOUNTer: a parsing tool to uncover the mature N-terminus of organelle-targeted proteins in complex samples. BMC Bioinformatics 18: 182

Linster E., et al (2015) Downregulation of N-terminal acetylation triggers ABA-mediated drought responses in Arabidopsis. Nat Commun 6: 7640

Xu F., et al (2015) Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis. Plant Cell 27: 1547-62

Dinh, T.V et al (2015) Molecular identification and functional characterization of the first Nα-acetyltransferase in plastids by a global acetylome profiling test, Proteomics, 15, 2426-2435

Bienvenut, W.V., et al (2012) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. Mol. Cell. Proteomics, 11: M111 015131

 

 

 

Publiée le
3 Fevrier 2020
Chargé de dossier
Giglione Carmela
Email du contact
Type de contrat
CDD
Lieu
I2BC
Rémunération
1600
A pourvoir pour
01.04.2020