Periplasmic domains define holin-antiholin interactions in T4 lysis inhibition

Journal of Bacteriology

Volumn 187, Issue 19, 2005, Pages 6631-6640

  Tran, Tram Anh T ^a   Struck, Douglas K ^a   Young, Ry ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOLYSIN E; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; PEPTIDOGLYCAN; POLYPEPTIDE; PROTEIN HOLIN; PROTEIN HOLIN T; UNCLASSIFIED DRUG;

ALLELE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE T4; CARBOXY TERMINAL SEQUENCE; CELL FRACTIONATION; CELL MEMBRANE; CHIMERA; COMPLEX FORMATION; CYTOPLASM; GENE; GENE EXPRESSION; GENE OVEREXPRESSION; LYSIS; MEMBRANE DAMAGE; MORPHOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN VARIANT; RI GENE; WILD TYPE;

AMINO ACID SEQUENCE; BACTERIOLYSIS; BACTERIOPHAGE T4; ENDOPEPTIDASES; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; PERIPLASMIC PROTEINS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; VIRAL PROTEINS;

EID: 25144505528     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.19.6631-6640.2005     Document Type: Article

References (39)

1. Abedon, S. T. 1994. Lysis and the interaction between free phages and infected cells, p. 397-405. In J. D. Karam, J. W. Drake, K. N. Kreuzer, G. Mosig, D. H. Hall, F. A. Eiserling, L. W. Black, E. K. Spicer, E. Kutter, K. Carlson, and E. S. Miller (ed.), Molecular biology of bacteriophage T4. American Society for Microbiology, Washington, D.C.
2. Bendtsen, J. D., H. Nielsen, G. von Heijne, and S. Brunak. 2004. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol 340:783-795.
3. Benzer, S. 1957. The elementary units of heredity, p. 70-93. In B. Glass (ed.), The chemical basis of heredity. The John Hopkins Press, Baltimore, Md.
4. Bläsi, U., C.-Y. Chang, M. T. Zagotta, K. Nam, and R. Young. 1990. The lethal λ S gene encodes its own inhibitor. EMBO J. 9:981-989.
5. Brock, T. D. 1990. The emergence of bacterial genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
6. Broome-Smith, J. K., and B. G. Spratt. 1986. A vector for the construction of translational fusions to TEM beta-lactamase and the analysis of protein export signals and membrane protein topology. Gene 49:341-349.
7. Cairns, J., G. S. Stent, and J. D. Watson. 1966. Phage and the origins of molecular biology. Cold Spring Harbor Laboratory of Quantitative Biology, Cold Spring Harbor, N.Y.
8. Doermann, A. H. 1948. Lysis and lysis inhibition with Escherichia coli bacteriophage. J. Bacteriol. 55:257-276.
9. Doermann, A. H. 1952. The intracellular growth of bacteriophages. 1. Liberation of intracellular bacteriophage T4 by premature lysis with another phage or with cyanide. J. Gen. Physiol. 35:645-656.
10. Dressman, H. K., and J. W. Drake. 1999. Lysis and lysis inhibition in bacteriophage T4: rV mutations reside in the holin τ gene. J. Bacteriol. 181: 4391-4396.
11. Graschopf, A., and U. Bläsi. 1999. Functional assembly of the lambda S holin requires periplasmic localization of its N-terminus. Arch. Microbiol. 172:31-39.
12. Graschopf, A., and U. Bläsi. 1999. Molecular function of the dual-start motif in the λ S holin. Mol. Microbiol. 33:569-582.
13. Gründling, A., U. Bläsi, and R. Young. 2000. Biochemical and genetic evidence for three transmembrane domains in the class I holin, λ S. J. Biol. Chem. 275:769-776.
14. Gründling, A., U. Bläsi, and R. Young. 2000. Genetic and biochemical analysis of dimer and oligomer interactions of the λ S holin. J. Bacteriol. 182:6082-6090.
15. Hershey, A. D. 1946. Mutation of bacteriophage with respect to type of plaque. Genetics 31:620-640.
16. Hershey, A. D. 1946. Spontaneous mutations in bacterial viruses. Cold Spring Harbor Symp. Quant. Biol. 11:67-77.
17. Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
18. Karam, J. D., J. W. Drake, K. N. Kreuzer, G. Mosig, D. H. Hall, F. A. Eiserling, L. W. Black, E. K. Spicer, E. Kutter, K. Carlson, and E. S. Miller. 1994. Molecular biology of bacteriophage T4. ASM Press, Washington, D.C.
19. Kolisnychenko, V., G. Plunkett III, C. D. Herring, T. Feher, J. Posfai, F. R. Blattner, and G. Posfai. 2002. Engineering a reduced Escherichia coli genome. Genome Res. 12:640-647.
20. Krylov, V. N. 1966. A new r gene of bacteriophage T4B? Microb. Genet. Bull. 24:4-5.
21. Krylov, V. N., and A. Zapadnaya. 1965. Bacteriophage T4B r mutations sensitive to temperature (rts). Genetika 1:7-11.
22. Los, M., G. Wegrzyn, and P. Neubauer. 2003. A role for bacteriophage T4 rI gene function in the control of phage development during pseudolysogeny and in slowly growing host cells. Res. Microbiol. 154:547-552.
23. Lu, M., and U. Henning. 1989. The immunity (imm) gene of Escherichia coli bacteriophage T4. J. Virol. 63:3472-3478.
24. Lu, M.-J., and U. Henning. 1994. Superinfection exclusion by T-even-type coliphages. Trends Microbiol. 2:137-139.
25. Lutz, R., and H. Bujard. 1997. Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/ 11-12 regulatory elements. Nucleic Acids Res. 25:1203-1210.
26. Matthews, B. W. 1996. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J. 10:35-41.
27. Paddison, P., S. T. Abedon, H. K. Dressman, K. Gailbreath, J. Tracy, E. Mosser, J. Neitzel, B. Guttman, and E. Kutter. 1998. The roles of the bacteriophage T4 r genes in lysis inhibition and fine-structure genetics: a new perspective. Genetics 148:1539-1550.
28. Raab, R., G. Neal, C. Sohaskey, J. Smith, and R. Young. 1988. Dominance in lambda S mutations and evidence for translational control. J. Mol. Biol. 199:95-105.
29. Ramanculov, E. R., and R. Young. 2001. An ancient player unmasked: T4 rI encodes a t-specific antiholin. Mol. Microbiol. 41:575-583.
30. Ramanculov, E. R., and R. Young. 2001. Functional analysis of the T4 t holin in a lambda context. Mol. Genet. Genomics 265:345-353.
31. Ramanculov, E. R., and R. Young. 2001. Genetic analysis of the T4 holin: timing and topology. Gene 265:25-36.
32. Shapira, A., E. Giberman, and A. Kohn. 1974. Recoverable potassium fluxes variations following adsorption of T4 phage and their ghosts on Escherichia coli B. J. Gen. Virol. 23:159-171.
33. Siegele, D. A., and J. C. Hu. 1997. Gene expression from plasmids containing the araBAD promoter at subsaturating inducer concentrations represents mixed populations. Proc. Natl. Acad. Sci. USA 94:8168-8172.
34. Wang, I. N., D. E. Dykhuizen, and L. B. Slobodkin. 1996. The evolution of phage lysis timing. Evol. Ecol. 10:545-558.
35. Wang, I. N., D. L. Smith, and R. Young. 2000. Holins: the protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54:799-825.
36. Xu, M., D. K. Struck, J. Deaton, I. N. Wang, and R. Young. 2004. The signal arrest-release (SAR) sequence mediates export and control of the phage P1 endolysin. Proc. Nat. Acad. Sci. USA 101:6415-6420.
37. Young, R. 1992. Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56:430-481.
38. Young, R. 2002. Bacteriophage holins: deadly diversity. J. Mol. Microbiol. Biotechnol. 4:21-36.
39. Young, R., I. N. Wang, and W. D. Roof. 2000. Phages will out: strategies of host cell lysis. Trends Microbiol. 8:120-128.