Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail

Anastasiia Chaban, Leonid Minakhin, Ekaterina Goldobina, Brain Bae, Yue Hao, Sergei Borukhov, Leena Putzeys, Maarten Boon, Florian Kabinger, Rob Lavigne, Kira S. Makarova, Eugene V. Koonin, Satish K. Nair (), Shunsuke Tagami (), Konstantin Severinov () and Maria L. Sokolova ()
Additional contact information
Anastasiia Chaban: Center of Life Sciences, Skolkovo Institute of Science and Technology
Leonid Minakhin: The State University of New Jersey
Ekaterina Goldobina: Center of Life Sciences, Skolkovo Institute of Science and Technology
Brain Bae: University of Illinois at Urbana−Champaign
Yue Hao: University of Illinois at Urbana−Champaign
Sergei Borukhov: Rowan University School of Osteopathic Medicine at Stratford
Leena Putzeys: Laboratory of Gene Technology, KU Leuven
Maarten Boon: Laboratory of Gene Technology, KU Leuven
Florian Kabinger: Max Planck Institute for Multidisciplinary Sciences
Rob Lavigne: Laboratory of Gene Technology, KU Leuven
Kira S. Makarova: National Institutes of Health
Eugene V. Koonin: National Institutes of Health
Satish K. Nair: University of Illinois at Urbana−Champaign
Shunsuke Tagami: RIKEN Center for Biosystems Dynamics Research
Konstantin Severinov: The State University of New Jersey
Maria L. Sokolova: Center of Life Sciences, Skolkovo Institute of Science and Technology

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Thermus thermophilus bacteriophage P23-45 encodes a giant 5,002-residue tail tape measure protein (TMP) that defines the length of its extraordinarily long tail. Here, we show that the N-terminal portion of P23-45 TMP is an unusual RNA polymerase (RNAP) homologous to cellular RNAPs. The TMP-fused virion RNAP transcribes pre-early phage genes, including a gene that encodes another, non-virion RNAP, that transcribes early and some middle phage genes. We report the crystal structures of both P23-45 RNAPs. The non-virion RNAP has a crab-claw-like architecture. By contrast, the virion RNAP adopts a unique flat structure without a clamp. Structure and sequence comparisons of the P23-45 RNAPs with other RNAPs suggest that, despite the extensive functional differences, the two P23-45 RNAPs originate from an ancient gene duplication in an ancestral phage. Our findings demonstrate striking adaptability of RNAPs that can be attained within a single virus species.

Date: 2024
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DOI: 10.1038/s41467-023-44630-z

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