Research assistant (Praedoc) (m/f/d) – Department of Biology, Chemistry, Pharmacy

Department of Biology, Chemistry, Pharmacy – Institute of Chemistry and Biochemistry

AG Absmeier

 

Research assistant (Praedoc) (m/f/d)

with 65%-part-time job

limited to 30.06.2028

salary grade (Entgeltgruppe) 13 TV-L FU

reference code: Absmeier_TRR186_EN

 

The Absmeier group https://www.bcp.fu-berlin.de/en/chemie/biochemie/research-groups/absmeier-group/index.html) is interested in the regulation of messenger RNA (mRNA) translation and decay. mRNA decay is an important mechanism to control gene expression. It ensures a dynamic and rapid translatome remodeling response upon developmental and environmental cues. The canonical mRNA decay pathway starts with the removal of the 3´ poly(A) tail by deadenylases, such as the CCR4-NOT complex. Targeted mRNA decay can be achieved by adaptor proteins, which bind specifically to an RNA and recruit the CCR4-NOT complex. The MEX3 proteins are such adaptor proteins, which contain in addition to the RNA binding domain an E3 ubiquitin ligase domain. MEX3 ubiquitinates the CNOT7/8 deadenylase subunit of the CCR4-NOT complex. This leads to enhanced mRNA decay, resulting in e.g. natural killer cell activation, or evasion of the immune system by cancer cells. The molecular details of how MEX3 proteins recruit CCR4-NOT to an mRNA and how CNOT7/8 ubiquitination stimulates mRNA decay are elusive to date. This position is subject to funding approval.

 

Job description:

A PhD position is available in the Absmeier group at Freie Universität Berlin in the project “The MEX3 protein family of RNA binding E3 ligases- a switch for controlling rapid mRNA decay”, which is part of the DFG funded TRR186 (Molecular switches in the spatio-temporal control of cellular signal transmission).

 

Requirements:

Completed university degree (Master) in biochemistry or related subjects.

 

Desirable:

Candidates are expected to have a good understanding and an experimental background in protein biochemistry and/or structural biology. The project involves the recombinant production of proteins and protein complexes (bacteria, insect cells), interaction studies between proteins and/or RNA, functional studies (e.g. in vitro deadenylation and ubiquitination assays) and structural studies. In addition, in cellulo studies will be performed to test e.g. results from structural and functional studies and to determine new interaction partners.

 

Advantageous skills:

* Molecular cloning (e.g. restriction-, Gibson cloning, site directed mutagenesis)

* Recombinant production of proteins and protein complexes in Escherichia coli and insect cells

* Purification of recombinant proteins with various methods

* Interaction studies for protein-protein interactions or protein-RNA interactions (e.g. analytical gelfiltration, pulldown)

* Experimental and theoretical background in structural biology (e.g. macromolecular crystallography, cryogenic electron microscopy, crosslinking mass-spectrometry)

* Experience in human cell culture

 

Applications should comprise study records, the name of two reviewers for letters of recommendation, a motivation letter, and a CV, stating the reference:

Absmeier_ TRR186_EN and are to be sent to eva.absmeier@fu-berlin.de.

For further information, please contact Dr. Eva Absmeier (eva.absmeier@fu-berlin.de/ 03083850508).

Applications should be sent by e-mail, together with significant documents, indicating the reference code, no later than July 8th, 2024 in PDF format (preferably as one document) to Ms. Dr. Eva Absmeier: eva.absmeier@fu-berlin.de or postal to

 

Freie Universität Berlin

Fachbereich Biologie, Chemie, Pharmazie

Institut für Chemie und Biochemie

AG Absmeier

Frau Dr. Eva Absmeier

Takustr. 6

14195 Berlin (Dahlem)

 

With an electronic application, you acknowledge that FU Berlin saves and processes your data. FU Berlin cannot guarantee the security of your personal data if you send your application over an unencrypted connection.

Freie Universität Berlin is an equal opportunity employer.