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Structure paper

TitleThe Structural Basis of T4 Phage Lysis Control: DNA as the Signal for Lysis Inhibition.
Journal, issue, pagesJ Mol Biol, Vol. 432, Issue 16, Page 4623-4636, Year 2020
Publish dateJul 24, 2020
AuthorsInna V Krieger / Vladimir Kuznetsov / Jeng-Yih Chang / Junjie Zhang / Samir H Moussa / Ryland F Young / James C Sacchettini /
PubMed AbstractOptimal phage propagation depends on the regulation of the lysis of the infected host cell. In T4 phage infection, lysis occurs when the holin protein (T) forms lesions in the host membrane. However, ...Optimal phage propagation depends on the regulation of the lysis of the infected host cell. In T4 phage infection, lysis occurs when the holin protein (T) forms lesions in the host membrane. However, the lethal function of T can be blocked by an antiholin (RI) during lysis inhibition (LIN). LIN sets if the infected cell undergoes superinfection, then the lysis is delayed until host/phage ratio becomes more favorable for the release of progeny. It has been thought that a signal derived from the superinfection is required to activate RI. Here we report structures that suggest a radically different model in which RI binds to T irrespective of superinfection, causing it to accumulate in a membrane as heterotetrameric 2RI-2T complex. Moreover, we show the complex binds non-specifically to DNA, suggesting that the gDNA from the superinfecting phage serves as the LIN signal and that stabilization of the complex by DNA binding is what defines LIN. Finally, we show that soluble domain of free RI crystallizes in a domain-swapped homotetramer, which likely works as a sink for RI molecules released from the RI-T complex to ensure efficient lysis. These results constitute the first structural basis and a new model not only for the historic LIN phenomenon but also for the temporal regulation of phage lysis in general.
External linksJ Mol Biol / PubMed:32562709 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.65 - 9.4 Å
Structure data

EMDB-22250:
The Heterotetramers of Holin-Antiholin
Method: EM (single particle) / Resolution: 9.4 Å

PDB-6psh:
Crystal structure of periplasmic domain of antiholin RI from T4 phage
Method: X-RAY DIFFRACTION / Resolution: 2.21 Å

PDB-6psk:
Crystal structure of the complex between periplasmic domains of antiholin RI and holin T from T4 phage, in P6522
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-6px4:
Crystal structure of the complex between periplasmic domains of antiholin RI and holin T from T4 phage, in H32
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6pxe:
Crystal structure of the complex between periplasmic domains of antiholin RI and holin T from T4 phage, in P21
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-BTB:
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-CL:
Unknown entry

Source
  • Escherichia phage T4 (virus)
  • enterobacteria phage t4 (virus)
  • escherichia phage ecml-134 (virus)
  • escherichia phage vb_ecom_nbg2 (virus)
KeywordsVIRAL PROTEIN / phage / lysis inhibition

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