Phages will out: Strategies of host cell lysis

Trends in Microbiology

Volumn 8, Issue 3, 2000, Pages 120-128

  Young, Ry ^a   Wang, Ing Nang ^a   Roof, William D ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE DNA; HYDROLASE; MEMBRANE PROTEIN; RNA; SINGLE STRANDED DNA;

BACTERIAL MEMBRANE; BACTERIOPHAGE; CELL CYCLE; CYTOLYSIS; HOST CELL; MEMBRANE PERMEABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; REVIEW;

AMINO ACID SEQUENCE; BACTERIOPHAGES; CELL MEMBRANE PERMEABILITY; ENDOPEPTIDASES; GRAM-NEGATIVE BACTERIA; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; VIRAL PROTEINS;

BACTERIA (MICROORGANISMS); UNIDENTIFIED BACTERIOPHAGE;

EID: 0034162940     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(00)01705-4     Document Type: Review

References (54)

1. Young, R. (1992) Bacteriophage lysis: Mechanism and regulation. Microbiol. Rev. 56, 430-481
2. Witte, A. et al. (1990) φX174 protein E-mediated lysis of Escherichia coli. Biochimie 72, 191-200
3. Walderich, B. et al. (1988) Induction of the autolytic system of Escherichia coli by specific insertion of bacteriophage MS2 lysis protein into the bacterial cell envelope. J. Bacteriol. 170, 5027-5033
4. Young, R. and Bläsi, U. (1995) Holins: Form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17, 191-205
5. Diaz, E. et al. (1996) The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in Gram-negative bacteria: Triggering of the major pneumococcal autolysin in Escherichia coli. Mol. Microbiol. 19, 667-681
6. Diaz, E. et al. (1989) Subcellular localization of the major pneumococcal autolysin: A peculiar mechanism of secretion in Escherichia coli. J. Biol. Chem. 264, 1238-1244
7. Loessner, M.J. et al. (1999) Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187. J. Bacteriol. 181, 4452-4460
8. Navarre, W.W. et al. (1999) Multiple enzymatic activities of the murein hydrolase from staphylococcal phage φ11. Identification of a D-alanyl-glycine endopeptidase activity. J. Biol. Chem. 274, 15847-15856
9. Steiner, M. et al. (1993) The missing link in phage lysis of Gram-positive bacteria: Gene 14 of Bacillus subtilis phage φ29 encodes the functional homolog of lambda S protein. J. Bacteriol. 175, 1038-1042
10. Bläsi, U. et al. (1999) The C-terminal sequence of the lambda holin constitutes a cytoplasmic regulatory domain. J. Bacteriol. 181, 2922-2929
11. Smith, D.L. et al. (1998) Purification and biochemical characterization of the lambda holin. J. Bacteriol. 180, 2531-2540
12. Graschopf, A. and Bläsi, U. (1999) Molecular function of the dual-start motif in the λ S holin. Mol. Microbiol. 33, 569-582
13. Gründling, A. et al. (1999) Biochemical and genetic evidence for three transmembrane domains in the class I holin, λ S. J. Biol. Chem. 275, 769-776
14. Zagotta, M.T. and Wilson, D.B. (1990) Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli. J. Bacteriol. 172, 912-921
15. Raab, R. et al. (1988) Dominance in lambda S mutations and evidence for translational control. J. Mol. Biol. 199, 95-105
16. Johnson-Boaz, R. et al. (1994) A dominant mutation in the bacteriophage lambda S gene causes premature lysis and an absolute defective plating phenotype. Mol. Microbiol. 13, 495-504
17. Bläsi, U. and Young, R. (1996) Two beginnings for a single purpose: The dual-start holins in the regulation of phage lysis. Mol. Microbiol. 21, 675-682
18. Cao, G. and Dalbey, R.E. (1994) Translocation of N-terminal tails across the plasma membrane. EMBO J. 13, 4662-4669
19. Dalbey, R.E. et al. (1995) Directionality in protein translocation across membranes: The N-tail phenomenon. Trends Cell Biol. 5, 380-383
20. Chang, C.-Y. et al. (1995) S gene expression and the timing of lysis by bacteriophage λ. J. Bacteriol. 177, 3283-3294
21. Reader, R.W. and Siminovitch, L. (1971) Lysis defective mutants of bacteriophage lambda: On the role of the S function in lysis. Virology 43, 623-637
22. Barenboim, M. et al. (1999) Characterization of the dual start motif of a class II holin gene. Mol. Microbiol. 32, 715-727
23. Ziermann, R. et al. (1994) Functions involved in bacteriophage P2-induced host cell lysis and identification of a new tail gene. J. Bacteriol. 176, 4974-4984
24. Schmidt, C. et al. (1996) Three functions of bacteriophage P1 involved in cell lysis. J. Bacteriol. 178, 1099-1104
25. Hershey, A.D. (1946) Mutation of bacteriophage with respect to type of plaque. Genetics 31, 620-640
26. Paddison, P. et al. (1998) The roles of the bacteriophage T4 r genes in lysis inhibition and fine-structure genetics: A new perspective. Genetics 148, 1539-1550
27. Dressman, H.K. and Drake, J.W. (1999) Lysis and lysis inhibition in bacteriophage T4: r V mutations reside in the holin t gene. J. Bacteriol. 181, 4391-4396
28. Kedzierska, S. et al. (1996) The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli. Gene 168, 1-8
29. Zhang, N. and Young, R. (1999) Complementation and characterization of the nested Rz and Rz1 reading frames. Mol. Gen. Genet. 262, 659-667
30. Taylor, A. (1971) Endopeptidase activity of phage λ endolysin. Nat. New Biol. 234, 144-145
31. Sanger, F. et al. (1977) Nucleotide sequence of bacteriophage φX174 DNA. Nature 265, 687
32. Atkins, J.F. et al. (1979) Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping gene encoding a lysis function. Cell 18, 247-256
33. Model, P. et al. (1979) Characterization of Op3, a lysis-defective mutant of bacteriophage f2. Cell 18, 235-244
34. 2) protein leads to cell lysis. Cell 33, 877-885
35. Young, K.D. and Young, R. (1982) Lytic action of cloned φX174 gene E. J. Virol. 44, 993-1002
36. Henrich, B. et al. (1982) Lysis of Escherichia coli by induction of cloned φX174 genes. Mol. Gen. Genet. 185, 493-497
37. Remault, E. et al. (1982) Functional expression of individual plasmid-coded RNA bacteriophage MS2 genes. EMBO J. 1, 205-209
38. Maratea, D. et al. (1985) Deletion and fusion analysis of the φX174 lysis gene E. Gene 40, 39-46
39. Buckley, K.J. and Hayashi, M. (1986) Lytic activity localized to membrane-spanning region of φX174 E protein. Mol. Gen. Genet. 204, 120-125
40. Roof, W.D. et al. (1994) slyD, a host gene required for φX174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases. J. Biol. Chem. 269, 2902-2910
41. Wülfing, C. et al. (1994) An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Cbem. 269, 2895-2901
42. Hottenrott, S. et al. (1997) The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis-trans-isomerase. J. Biol. Chem. 272, 15697-15701
43. Mitterauer, T. et al. (1999) Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD. Biochem. J. 342, 33-39
44. Scholz, C. et al. (1999) R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays. FEBS Lett. 443, 367-369
45. Witte, A. et al. (1998) Mutations in cell division proteins FtsZ and FtsA inhibit φX174-protein-E-mediated lysis of Escherichia coli. Arch. Microbiol. 170, 259-268
46. Bradley, D.E. et al. (1969) Structural changes in Escherichia coli infected with a φX174-type bacteriophage. J. Gen. Virol. 5, 113-121
47. Gschwender, H.H. and Hofschneider, P.H. (1969) Lysis inhibition of φX174, MS2, and Qβ-infected Escherichia coli bacteria by magnesium ions. Biochim. Biophys. Acta 190, 454-459
48. Lubitz, W. et al. (1984) Requirement for a functional host cell autolytic enzyme system for lysis of Escherichia coli by bacteriophage φX174. J. Bacteriol. 159, 385-387
49. Lubitz, W. et al. (1984) Lysis of Escherichia coli after infection with φX174 depends on the regulation of the cellular autolytic system. J. Gen. Microbiol. 130, 1079-1087
50. Witte, A. et al. (1997) Proline 21, a residue within the α helical domain of φX174 lysis protein E, is required for its function in Escherichia coli. Mol. Microbiol. 26, 337-346
51. Bernhardt, T.G. et al. Genetic evidence that the bacteriophage φX174 lysis protein inhibits cell wall synthesis. Proc. Natl. Acad. Sci. U. S. A. (in press)
52. Ikeda, M. et al. (1991) The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: Undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase. J. Bacteriol. 173, 1021-1026
53. Brunskill, E.W. and Bayles, K.W. (1996) Identification of LytSR-regulated genes from Staphylococcus aureus. J. Bacteriol. 178, 5810-5812
54. Kawarabayasi, Y. et al. (1998) Complete sequence and gene organization of the genome of a hyper-thermophilic arachaebacterium, Pyrococcus horikoshii OT3. DNA Res. 5, 55-76