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PMID:15090650
| Citation |
Xu, M, Struck, DK, Deaton, J, Wang, IN and Young, R (2004) A signal-arrest-release sequence mediates export and control of the phage P1 endolysin. Proc. Natl. Acad. Sci. U.S.A. 101:6415-20 |
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| Abstract |
The Lyz endolysin of bacteriophage P1 was found to cause lysis of the host without a holin. Induction of a plasmid-cloned lyz resulted in lysis, and the lytic event could be triggered prematurely by treatments that dissipate the proton-motive force. Instead of requiring a holin, export was mediated by an N-terminal transmembrane domain (TMD) and required host sec function. Exported Lyz of identical SDS/PAGE mobility was found in both the membrane and periplasmic compartments, indicating that periplasmic Lyz was not generated by the proteolytic cleavage of the membrane-associated form. In gene fusion experiments, the Lyz TMD directed PhoA to both the membrane and periplasmic compartments, whereas the TMD of the integral membrane protein FtsI restricts Lyz to the membrane. Thus, the N-terminal domain of Lyz is both necessary and sufficient not only for export of this endolysin to the membrane but also for its release into the periplasm. The unusual N-terminal domain, rich in residues that are weakly hydrophobic, thus functions as a signal-arrest-release sequence, which first acts as a normal signal-arrest domain to direct the endolysin to the periplasm in membrane-tethered form and then allows it to be released as a soluble active enzyme in the periplasm. Examination of the protein sequences of related bacteriophage endolysins suggests that the presence of an N-terminal signal-arrest-release sequence is not unique to Lyz. These observations are discussed in relation to the role of holins in the control of host lysis by bacteriophage encoding a secretory endolysin. |
| Links |
PubMed PMC404059 Online version:10.1073/pnas.0400957101 |
| Keywords |
Amino Acid Sequence; Bacteriophage P1/metabolism; Endopeptidases/chemistry; Endopeptidases/metabolism; Escherichia coli/virology; Molecular Sequence Data; Protein Sorting Signals; Protein Transport; Sequence Homology, Amino Acid; Subcellular Fractions |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0019835: cytolysis |
ECO:0007699: cell growth assay evidence used in manual assertion |
P |
Fig. 1A shows culture clearing after induction of recombinant Lys in XL1-Blue cells. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin |
complete | ||||
| GO:0042597: periplasmic space |
ECO:0006042: cell fractionation evidence used in manual assertion |
C |
Fig. 3B shows presence of Lyz in periplasmic fractions. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin |
complete | ||||
| GO:0033646: host intracellular part |
ECO:0006042: cell fractionation evidence used in manual assertion |
C |
Fig. 3 shows presence of Lyz in soluble fraction. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin |
complete | ||||
| GO:0033644: host cell membrane |
ECO:0006042: cell fractionation evidence used in manual assertion |
C |
Fig. 3 shows presence of Lyz in membrane fraction. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin |
complete | ||||
See also
References
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