9RJS

Structure of the Bacteriophage PhiKZ non-virion RNA Polymerase bound to an analogue of its promoter

Summary for 9RJS

• Entry DOI: 10.2210/pdb9rjs/pdb
• Related: 7OGP 7OGR 8QUE
• EMDB information: 54012
• Descriptor: DNA-directed RNA polymerase,PHIKZ056.1, PHIKZ068, PHIKZ071, ... (8 entities in total)
• Functional Keywords: phikz, nvrnap, rna, dna, transcription, rna binding protein
• Biological source: Phikzvirus phiKZ; More
• Total number of polymer chains: 7
• Total formula weight: 382903.92

Authors

Chen, C.,de Martin Garrido, N.,Yakunina, M.,Aylett, C.H.S. (deposition date: 2025-06-12, release date: 2025-07-16)

Primary citation

de Martin Garrido, N.,Chen, C.S.,Ramlaul, K.,Aylett, C.H.S.,Yakunina, M.
Structure of the Bacteriophage PhiKZ Non-virion RNA Polymerase Transcribing from its Promoter p119L.
J.Mol.Biol., 436:168713-168713, 2024

PubMed Abstract: Bacteriophage ΦKZ (PhiKZ) is the founding member of a family of giant bacterial viruses. It has potential as a therapeutic as its host, Pseudomonas aeruginosa, kills tens of thousands of people worldwide each year. ΦKZ infection is independent of the host transcriptional apparatus; the virus forms a "nucleus", producing a proteinaceous barrier around the ΦKZ genome that excludes the host immune systems. It expresses its own non-canonical multi-subunit non-virion RNA polymerase (nvRNAP), which is imported into its "nucleus" to transcribe viral genes. The ΦKZ nvRNAP is formed by four polypeptides representing homologues of the eubacterial β/β' subunits, and a fifth that is likely to have evolved from an ancestral homologue to σ-factor. We have resolved the structure of the ΦKZ nvRNAP initiating transcription from its cognate promoter, p119L, including previously disordered regions. Our results shed light on the similarities and differences between ΦKZ nvRNAP mechanisms of transcription and those of canonical eubacterial RNAPs and the related non-canonical nvRNAP of bacteriophage AR9.

PubMed: 39029888
DOI: 10.1016/j.jmb.2024.168713

Experimental method

ELECTRON MICROSCOPY (2.59 Å)