John Prensner

@johnprensner.bsky.social

Pediatric neuro-oncologist, Asst Prof U-Michigan | Cancer researcher | RNA & ribosome enthusiast | Broad Institute, DFCI alum | book & music & tea lover | Dad | Views are mine (he/him). https://prensnerlab.org

Combined Optical Pooled Screens and Perturb-seq! Great new work by Romain Lopez & Taka Kudo. This is one of a series of papers from our lab (here, with Aviv Regev) using perturbations to interpret human genetics; a key revelation for me is how transferable the mouse perturbs are to human genetics.

Romain Lopez@biologicalml.org · 2mo ago

🚀 We are introducing PerturbPair (with Taka Kudo) — a platform that combines parallel Perturb-seq and optical pooled screening (PerturbView) in primary cells to systematically map at massive scale how genetic perturbations reshape cellular states across modalities. www.biorxiv.org/content/10.6...

🦠💡 Bacteria have millions of secret weapons against viruses! Researchers used AI to uncover millions of new bacterial proteins likely involved in antiviral defense — suggesting immunity genes make up ~1.5% of the genome, 3× more than thought. 🔗 www.pasteur.fr/en/research-... @audeber.bsky.social

Bacteria Have Millions of Secret Weapons Against Viruses

Millions of new proteins with predicted roles in defence against viruses have been identified in bacteria. It was thought that around 0.5% of the average bacterial genome had some involvement in immun...

pasteur.fr

Introducing peptidiens! Congratulations to the TransCODE consortium on this exciting tour-de-force in @nature.com: nature.com/articles/s41... We look forward to seeing what’s next as lead authors Sebastiaan van Heesch and John Prensner take on our dark proteome challenge as part of team ILLUMINE!

Expanding the human proteome with microproteins and peptideins - Nature

A large-scale proteomics analysis of the dark proteome by the TransCODE Consortium reveals many translated non-canonical open reading frames to encode microproteins and peptideins.

nature.com

Systematic analysis of C-termini of small open reading frame-encoded peptides. #Riboseq #proteomics #darkproteome pubs.acs.org/doi/10.1021/...

Systematic Analysis of C-Termini of Small Open Reading Frame-Encoded Peptides in Human Cancer Cell Lines

The C-termini often regulate protein biological functions through specific structures or modifications. Small open reading frame-encoded peptides (SEPs) make up a novel class of gene expression products that participate in various biological activities. Their C-termini have also been found to affect their function, but the polymorphism of SEPs’ C-termini has not yet been systematically elucidated. Using C-terminal proteomics, we identified 3636 C-terminal peptides from 2168 proteins in three human cancer cell lines, including 3364 peptides from 1901 classical proteins and 272 peptides from 267 SEPs. Approximately 20% of all of the identified C-terminal peptides had been reported in previous studies, originating from mRNA alternative splicing or protease cleavage, while more than 85% of the C-terminal peptides from SEPs were novel. Bioinformatics analysis revealed that most new SEP C-termini are likely produced by protease cleavage by the KLK, MMP, and CAT protease families. Others without accurately predicted hydrolysis sites may originate from alternative splicing or protein trimming. The intact and hydrolysis products of some SEPs were verified by immunoblotting. Some cleavage occurs in the predicted domain, which might affect SEPs’ function. This study enriches the SEP sequence information, provides experimental evidence for SEP in vivo processing, and supports the subsequent functional analysis of SEP.

pubs.acs.org