Alexandra Teslenko

@alexateslenko.bsky.social

Postdoctoral Researcher👩‍🔬@CeTPD, Alessio Ciulli Lab, Dundee 🇬🇧 Biophysical Chemistry | Chemical and Structural Biology | Drug Discovery

Excited to share our latest: we engineered the reactivity of a bacterial E1-like enzyme for ATP-driven modification of C termini. Our tool mimics the logic of peptide bond formation in biology for precision modification of proteins in vitro. 🧪https://rdcu.be/ewN7C

Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini

Nature Chemistry - In living systems, ATP provides an energetic driving force for protein synthesis and modification. Now, an engineered enzymatic tool has been developed for high-yield, ATP-driven...

rdcu.be

Our new study of chromatin ubiquitylation by variant PRC1 on the single-molecule scale: We visualize directly how vPRC1 ubiquitylates neighboring nucleosomes during a single binding event, showing a potential mechanism how H2Aub domains are established. www.science.org/doi/10.1126/...

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes

Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

science.org

There are days in life that shake you. I’m shattered 💔 to share that I just found out that the US Government terminated my 2024 NIH Director’s Early Independence Award (~$2 million), threatening my long-promised assistant professor job at Columbia University & academic career... 1/🧵

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🥳 Today we celebrated the PhD defense of our very first PhD student Kevin Schiefelbein 🤩 Kevin told us about his Lasso Peptide journey over the past four years, and it was so great to see the full story coming together. Congratulations Kevin, and thank you for everything! #proudPI

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We did this crazy project where we tried to see if proteins could interact with their mirror image ligand. Seems impossible when proteins need to form 3D structures to interact. But what about if the interaction remains disordered??? www.nature.com/articles/s41...

Stereochemistry in the disorder–order continuum of protein interactions - Nature

Studies on protein–protein interactions using proteins containing d- or l-amino acids show that stereoselectivity of binding varies with the degree of disorder within the complex.

nature.com

Please see our paper in Nature on read-write mechanisms of H2AK119 ubiquitination by Polycomb repressive complex I. Congrats to the whole team, especially Victoria and huge thanks to our collaborator JP Armache! Also big thanks to Mark Foundation for Cancer Research for the support! rdcu.be/dZ5HZ

Read–write mechanisms of H2A ubiquitination by Polycomb repressive complex 1

Nature - Cryo-electron microscopy and biochemical studies elucidate the read–write mechanisms of non-canonical PRC1-containing RYBP in histone H2A lysine 119 monoubiquitination and their...

rdcu.be