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PMID:22742425

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Citation

Tanaka, S and Clemons, WM Jr (2012) Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174. Mol. Microbiol. 85:975-85

Abstract

The DNA phage ΦX174 encodes the integral membrane protein E whose expression leads to host cell lysis by inhibition of the peptidoglycan synthesis enzyme MraY. Here we use mutagenesis to characterize the molecular details of the E lysis mechanism. We find that a minimal 18-residue region with the modified wild-type sequences of the conserved transmembrane helix of E is sufficient to lyse host cells and that specific residues within and at the boundaries of this helix are important for activity. This suggests that positioning of the helix in the membrane is critical for interactions with MraY. We further characterize the interaction site of the transmembrane helix with MraY demonstrating E forms a stable complex with MraY. Triggering cell lysis by peptidoglycan synthesis inhibition is a traditional route for antimicrobial strategies. Understanding the mechanism of bacterial cell lysis by E will provide insights into new antimicrobial strategies using re-engineered E peptides.

Links

PubMed PMC3429702 Online version:10.1111/j.1365-2958.2012.08153.x

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

BPPHS:E

GO:0019077: lytic viral release

ECO:0000315:

P

Figure 2A

complete
CACAO 5438

BPPHS:E

involved_in

GO:0044659: cytolysis by virus of host cell

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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