@SternbergLab
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News from the Sternberg lab at Columbia Univ., HHMI. Posts are from lab members and not Samuel Sternberg unless signed SHS. Posts represent personal views only.
New York, NY
Joined October 2017
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1/13 — New pre-print from the Sternberg Lab in collaboration with Leifu Chang's Lab! TnpB nucleases have repeatedly given rise to TldRs, nuclease-dead RNA-guided transcription factors. Here we define the biological role of a TldR clade in its native host.
biorxiv.org/content/10.64898…
12/13 — TldR is a naturally evolved parallel to engineered CRISPRi. Repression of an OppA variant shifts the relative contribution of remaining paralogs, which could influence which peptides a cell imports. What induces TldR natively remains unknown.
biorxiv.org/content/10.64898…
Just published! IStrons are a unique class of transposable elements that pack three distinct functions in one sequence. Here, we used pooled library mutagenesis and high-throughput sequencing to systematically map the sequence and structural features that govern these functions.
Link to paper!
academic.oup.com/nar/article…
Link to post with preprint
nitter.cf/SternbergLab/status/20…
New preprint from the Sternberg lab!
biorxiv.org/content/10.64898…
We used pooled oligonucleotide library mutagenesis + high-throughput sequencing to systematically dissect the molecular determinants of IStron transposition, RNA-guided DNA cleavage, and self-splicing.
Out now! In collaboration with Hiroshi Nishimasu's lab, we uncover how a dual reverse transcriptase immune system builds double-stranded DNA from both RNA and protein templates.
sciencedirect.com/science/ar…
Previous thread for the preprint: nitter.cf/SternbergLab/status/20…
1/9 New preprint from the Sternberg Lab in collaboration with the Nishimasu Lab! We uncover how the DRT3 antiphage immune system pairs two reverse transcriptases, one RNA-templated and one protein-templated, to build a double-stranded DNA effector. doi.org/10.64898/2026.05.04.…
1/11 New preprint from the Sternberg lab in collaboration with the Fernández lab! We are excited to share our structure-function study of DRT10, a bacterial defense-associated reverse transcriptase that synthesizes long tandem-repeat DNA.🧵
More here: biorxiv.org/content/10.64898…
10/11 This suggests a shared architectural logic underlying RNA-guided, tandem-repeat DNA synthesis across diverse bacterial Class 2 DRT systems & suggests that DRT10 is a structurally minimal version of the same strategy used by eukaryotic telomerase to achieve repeat addition.
11/11 Many thanks to all authors for their collective efforts in bringing this story to life! And a special thanks to @shsternberg and @IsraelF96135088 for their mentorship and support throughout this project.