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

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 vi...

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Bibliographic Details
Published in:	Nature communications Vol. 15; no. 1; p. 317
Main Authors:	Chaban, Anastasiia, Minakhin, Leonid, Goldobina, Ekaterina, Bae, Brain, Hao, Yue, Borukhov, Sergei, Putzeys, Leena, Boon, Maarten, Kabinger, Florian, Lavigne, Rob, Makarova, Kira S., Koonin, Eugene V., Nair, Satish K., Tagami, Shunsuke, Severinov, Konstantin, Sokolova, Maria L.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 05-01-2024 Nature Publishing Group Nature Portfolio
Subjects:	38 38/15 49/91 631/326/1321 631/337/572 631/45/535/1266 82/1 82/16 82/80 82/83 96 Adaptability Bacterial Typing Techniques Bacteriophages - genetics DNA-directed RNA polymerase DNA-Directed RNA Polymerases - genetics Gene duplication Genes Humanities and Social Sciences multidisciplinary Phages Proteins Pyridinolcarbamate Ribonucleic acid RNA RNA polymerase Science Science (multidisciplinary) Structure-function relationships Virion - genetics Virions Viruses
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Summary:	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. The authors describe the structure and function of two evolutionarily diverged RNA polymerases of a thermophilic phage. One of the polymerases is fused to the phage tape measure protein, a virion component dictating the length of the phage tail.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2041-1723 2041-1723
DOI:	10.1038/s41467-023-44630-z