Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits

Abstract

Background: Kil peptide from bacteriophage targets FtsZ to prevent host cell division. Results: Kil disrupts FtsZ protofilaments producing shorter oligomers of variable size with reduced GTPase activity. Conclusion: At high concentrations, Kil likely inhibits FtsZ assembly via a subunit sequestration mechanism. Significance: This is the first biophysical study of how a bacteriophage disruptor of bacterial division inhibits FtsZ assembly.

Splitsville: structural and functional insights into the dynamic bacterial Z ring

“…In addition, there has been a recent resurgence in understanding how bacteriophage factors alter host cell shape and division. For example, the E. coli phages T7 and λ produce peptides that inhibit host cell division during lytic growth by targeting FtsZ assembly 141–143 . In contrast, the B. subtilis phage φ29 binds to FtsZ but does not inhibit its function 144 .…”

OxyS small RNA induces cell cycle arrest to allow DNA damage repair

“…Assembly of the essential, tubulin‐like FtsZ protein into a ring‐shaped structure at the nascent division site serves as a scaffold for recruitment of the cell division machinery. Kil proteins prevent cell division by interfering with FtsZ function (Conter et al , ; Burke et al , ; Haeusser et al , ; Hernandez‐Rocamora et al , ). To determine whether recovery is due to interference with cell division, we examined growth resumption in cells with an intact oxyS allele and mild overexpression of ftsQAZ operon encoding ftsQ , ftsA, and ftsZ genes from a low‐copy plasmid (Bernhardt & de Boer, ).…”

“…Assembly of the essential, tubulin-like FtsZ protein into a ringshaped structure at the nascent division site serves as a scaffold for recruitment of the cell division machinery. Kil proteins prevent cell division by interfering with FtsZ function (Conter et al, 1996;Burke et al, 2013;Haeusser et al, 2014;Hernandez-Rocamora et al, 2015).…”

Purification and characterization of FtsZ from the citrus canker pathogen Xanthomonas citri subsp. citri

“…It is interesting that there was no decrease in the activity at low FtsZ concentration and the extrapolated x ‐intercept is very close to 0. This suggests a very low apparent critical concentration compared to FtsZ proteins from different species, which is normally in the range of 1–3 μ M (Chen, Milam, & Erickson, ; Hernández‐Rocamora, Alfonso, Margolin, Zorrilla, & Rivas, ; Mukherjee & Lutkenhaus, ; Oliva et al., ; White et al., ; Yang et al., ). The type of buffer (TRIS50 or HEPES7.5_50) and magnesium concentration (5–10 mM) did not influence XacFtsZ activity significantly (data not shown).…”