Eilika Weber-Ban (0000-0002-5773-9274)

Personal information

Biography

Eilika Weber-Ban is Professor at the Institute for Molecular Biology & Biophysics of the ETH Zurich. With her group she studies the molecular mechanisms involved in the maintenance of protein homeostasis in mycobacteria with a particular emphasis on the role played by large, multi-subunit degradation machines.
Eilika Weber-Ban studied Biochemistry as an undergraduate at the University of Tübingen. With a Fulbright-Scholarship she joined the graduate program of the University of California at Riverside, where she obtained a PhD degree in Biochemistry in 1996. After completion of her PhD studies, she was awarded a Jane-Coffin-Childs Postdoctoral Fellowship to work at Yale University with Prof. Arthur Horwich. In 2000 she joined the Institute of Molecular Biology & Biophysics at the ETH Zurich to establish her own research group.

Activities

Collapse all

ETH-Bereich Hochschulen: Zurich, ZH, CH

2000-09-01 to present | Principle Investigator (Biologie)

Employment

Eilika Weber-Ban

https://orcid.org/0000-0002-5773-9274

Personal information

Websites & social links

Other IDs

Keywords

Countries

Biography

Activities

Employment (2)

ETH-Bereich Hochschulen: Zurich, ZH, CH

Yale University School of Medicine: New Haven, CT, US

Education and qualifications (3)

University of California Riverside: Riverside, CA, US

University of California Riverside: Riverside, CA, US

Eberhard Karls Universität Tübingen: Tubingen, Baden-Württemberg, DE

Professional activities (1)

European Molecular Biology Organization: Heidelberg, DE

Works (50 of 69)

Single-Stranded DNA Binding to the Transcription Factor PafBC Triggers the Mycobacterial DNA Damage Response

In situ analysis of osmolyte mechanisms of proteome thermal stabilization

Publisher Correction: Novel WYL domain-containing transcriptional activator acts in response to genotoxic stress in rapidly growing mycobacteria

Novel WYL domain-containing transcriptional activator acts in response to genotoxic stress in rapidly growing mycobacteria

ATP-independent substrate recruitment to proteasomal degradation in mycobacteria

An emerging class of nucleic acid-sensing regulators in bacteria: WYL domain-containing proteins

Electrostatic interactions guide substrate recognition of the prokaryotic ubiquitin-like protein ligase PafA

ClpC2 protects mycobacteria against a natural antibiotic targeting ClpC1-dependent protein degradation

Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex

Transcriptional control of mycobacterial DNA damage response by sigma adaptation

Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation

Genome‐wide interaction screen for Mycobacterium tuberculosis ClpCP protease reveals toxin–antitoxin systems as a major substrate class

Protein post-translational modifications in bacteria

Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC

Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation

The Mycobacterial LexA/RecA-Independent DNA Damage Response Is Controlled by PafBC and the Pup-Proteasome System

Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms

Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes.

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response.

Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis.

Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins.

Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome.

The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1.

Pupylation-dependent and -independent proteasomal degradation in mycobacteria.

Bacterial proteasome activator bpa (rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome.

Chaperone-Proteases of Mycobacteria

Pupylation as a signal for proteasomal degradation in bacteria.

Crystal structure of the complex between prokaryotic ubiquitin-like protein and its ligase PafA.

FixK₂, a key regulator in Bradyrhizobium japonicum, is a substrate for the protease ClpAP in vitro.

Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway.

The pupylation pathway and its role in mycobacteria.

Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation.

Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate.

Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins.

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway.

Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate.

The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus.

Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo.

Both ATPase domains of ClpA are critical for processing of stable protein structures.

Clp chaperone-proteases: structure and function.

Studying chaperone-proteases using a real-time approach based on FRET.

A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa.

The alternating power stroke of a 6-cylinder AAA protease chaperone engine.

Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes.

Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes.

Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry.

Intersubunit cross-talk in pyridoxal 5'-phosphate synthase, coordinated by the C terminus of the synthase subunit.

An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity.

Structural basis of enzyme encapsulation into a bacterial nanocompartment.

The flexible attachment of the N-domains to the ClpA ring body allows their use on demand.