Structural highlights
Publication Abstract from PubMed
7-deazapurines are nucleobase analogs essential for nucleic acid modifications in nearly all cellular life. Here, we discover a role for 7-deazapurines in protein modification within type IV CBASS anti-phage defense and define functions for CBASS ancillary proteins Cap9 and Cap10 in nucleobase-protein conjugation. A structure of Cap10 reveals a tRNA transglycosylase-family enzyme remodeled to bind the modified N-terminus of a partner cGAS/DncV-like nucleotidyltransferase linked to a 7-amido-7-deazaguanine (NDG) nucleobase. The structure of Cap9 explains how this QueC-like enzyme co-opts a 7-deazapurine biosynthetic reaction mechanism for NDG conjugation. We demonstrate that Cap9, Cap10, and NDG conjugation are essential for host defense against phage infection. Our results define a previously unknown 7-deazapurine protein modification and explain how nucleobase biosynthetic machinery has been repurposed for antiviral immunity.
Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity.,Wassarman DR, Pfaff P, Paulo JA, Gygi SP, Shokat KM, Kranzusch PJ bioRxiv [Preprint]. 2025 Apr 6:2025.04.06.647259. doi: 10.1101/2025.04.06.647259. PMID:40236162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wassarman DR, Pfaff P, Paulo JA, Gygi SP, Shokat KM, Kranzusch PJ. Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity. bioRxiv [Preprint]. 2025 Apr 6:2025.04.06.647259. PMID:40236162 doi:10.1101/2025.04.06.647259
