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OLD amputates the anticodon arm of tRNAs during P2-Lambda interference.

Apurva A Govande1, Brian D Matibag1, Irem Ünlü1

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Overcoming Lysogenization Defect (OLD) proteins, like P2-OLD, degrade specific host tRNAs, causing cell death. Phage tRNAs with altered motifs resist this cleavage, resolving a long-standing phage conflict mystery.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • ATPase-coupled Toprim (Topoisomerase-primase) nucleases, known as Overcoming Lysogenization Defect (OLD) proteins, are vital for antiphage defenses.
  • P2-OLD protein, discovered in 1970, mediates P2-Lambda phage interference by halting Lambda replication in P2 prophage-carrying cells.

Purpose of the Study:

  • To elucidate the mechanism by which P2-OLD protein induces cell death.
  • To identify the specific molecular target of P2-OLD.
  • To understand the basis of P2-Lambda interference.

Main Methods:

  • Biochemical assays to identify P2-OLD targets.
  • RNA sequencing and analysis to characterize cleaved tRNAs.
  • Structural analysis of tRNA motifs recognized by P2-OLD.

Main Results:

  • P2-OLD specifically degrades host threonyl-tRNA with the UGU anticodon (tRNAThrU).
  • Cleavage occurs at a pseudo-palindromic CNG motif in the anticodon stem, resulting in anticodon arm amputation.
  • Phage threonyl-tRNAs resist cleavage due to altered CNG motifs and shorter anticodon stems, while host repair systems cannot restore cleaved tRNAs.

Conclusions:

  • P2-OLD employs a novel tRNA inactivation mechanism involving anticodon arm amputation.
  • This mechanism explains P2-Lambda interference and provides insights into Toprim nuclease specificity.
  • The findings resolve a long-standing mystery in phage-host interactions.