The C-terminal sequence of the λ holin constitutes a cytoplasmic regulatory domain

Journal of Bacteriology

Volumn 181, Issue 9, 1999, Pages 2922-2929

  Bläsi, Udo ^a   Fraisl, Peter ^a   Chang, Chung Yu ^b,c   Zhang, Ning ^b   Young, R Y ^b  

^a Vienna Biocenter   (Austria)

^b TEXAS A AND M UNIVERSITY   (United States)

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; GENE PRODUCT;

ARTICLE; BACTERIOPHAGE; CYTOPLASM; ESCHERICHIA COLI; GENE MUTATION; LYSIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PHENOTYPE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037513862     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.9.2922-2929.1999     Document Type: Article

References (42)

1. Barenboim, M., C.-Y. Chang, F. dib Hajj, and R. Young. A holin and its inhibitor are both encoded by the phage 21 S gene. Mol. Microbiol., in press.
2. Bienkowska-Szewczyk, K., B. Lipinska, and A. Taylor. 1981. The R gene product of bacteriophage λ is the murein transglycosylase. Mol. Gen. Genet. 184:111-114.
3. Bläsi, U., C.-Y. Chang, and R. Young. Unpublished data.
4. Bläsi, U., C.-Y. Chang, M. T. Zagotta, K. Nam, and R. Young. 1990. The lethal λ 5 gene encodes its own inhibitor. EMBO J. 9:981-989.
5. Bläsi, U., K. Nam, D. Hartz, L. Gold, and R. Young. 1989. Dual translational initiation sites control function of the λ 5 gene. EMBO J. 8:3501-3510.
6. Bläsi, U., and R. Young. 1996. Two beginnings for a single purpose: the dual-start holins in the regulation of phage lysis. Mol. Microbiol. 21:675-682.
7. Bonovich, M. T., and R. Young. 1991. Dual start motif in two lambdoid S genes unrelated to λ S. J. Bacteriol. 173:2897-2905.
8. Casjens, S. R., K. Eppler, R. Parr, and A. R. Poteete. 1989. Nucleotide sequence of the bacteriophage P22 gene 19 to 3 region: identification of a new gene required for lysis. Virology 171:588-598.
9. Chang, C-Y., K. Nam, U. Bläsi, and R. Young. 1993. Synthesis of two bacteriophage λ S proteins in an in vivo system. Gene 133:9-16.
10. Chang, C.-Y., K. Nam, and H. Young. 1995. S gene expression and the timing of lysis by bacteriophage λ. J. Bacteriol. 177:3283-3294.
11. Cheng, X., X. Zhang, J. W. Pflugrath, and F. W. Studier. 1994. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 91:4034-4038.
12. Forbes, D., and I. Herskowitz. 1982. Polarity suppression by the Q gene product of phage lambda. J. Mol. Biol. 160:549-569.
13. Fraisl, P., and R. Young. Unpublished data.
14. Gafvelin, G., and G. von Heijne. 1994. Topological "frustration" in multispanning E. coli inner membrane proteins. Cell 77:401-412.
15. Geller, B. L. 1990. Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli. J. Bacteriol. 172:4870-4876.
16. Goldberg, A. R., and M. Howe. 1969. New mutations in the S cistron of bacteriophage lambda affecting host cell lysis. Virology 38:200-202.
17. Graschopf, A., and U. Bläsi. Molecular function of the dual-start motif in the lambda S holin. Submitted for publication.
18. Gründling, A., and R. Young. Unpublished data.
19. Hendrix, R. 1992. Personal communication.
20. Itakura, K., T. Hirose, R. Crea, A. Riggs, H. L. Heyneker, F. Boliver, and H. W. Boyer. 1979. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 198:1056-1063.
21. Johnson-Boaz, R., C.-V. Chang, and R. Young. 1994. A dominant mutation in the bacteriophage lambda S gene causes premature lysis and an absolute defective plating phenotype. Mol. Microbiol. 13:495-504.
22. Kuhn, A., H.-Y. Zhu, and R. E. Dalbey. 1990. Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion. EMBO J. 9:2385-2389.
23. Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-382.
24. Lemmon, M. A., J. M. Flanagan, H. R. Treutlein, J. Zhang, and D. M. Engelman. 1992. Sequence specificity in the dimerization of transmembrane alpha-helices. Biochemistry 31:12719-12725.
25. Messing, J., R. Crea, and P. H. Seeburg. 1981. A system for shotgun DNA sequencing. Nucleic Acids Res. 9:309-321.
26. Miller, J. H. 1992. A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
27. Müller, M., and G. Blobel. 1984. In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 81:7421-7425.
28. Nam, K., U. Bläsi, M. T. Zagotta, and R. Young. 1990. Conservation of a dual-start motif in P22 lysis gene regulation. J. Bacteriol. 72:204-211.
29. Pontarollo, R. A., C. R. Rioux, and A. A. Potter. 1997. Goning and characterization of bacteriophage-like DNA from Haemophilus somnus homologous to phages P2 and HP1. J. Bacteriol. 179:1872-1879.
30. Raab, R., G. Neal, J. Garrett, R. Grimaila, R. Fusselman, and R. Young. 1986. Mutational analysis of bacteriophage lambda lysis gene S. J. Bacteriol. 167:1035-1042.
31. 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,
32. Reader, R. W., and L. Siminovitch. 1971. Lysis defective mutants of bacteriophage lambda: on the role of the S function in lysis. Virology 43:623-637.
33. Silhavy, T. J., M. L. Berman, and L. W. Enquist. 1984. Experiments with gene fusions. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
34. Smith, D. L., D. K. Struck, J. M. Scboltz, and R. Young. 1998. Purification and biochemical characterization of the lambda holin. J. Bacteriol. 180:2531-2540.
35. Smith, D. L., and R. Young. 1998. Oligohistidine tag mutagenesis of the λ holin gene. J. Bacteriol. 180:4199-4211.
36. Steiner, M., and U. Bläsi. 1993. Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105. Mol. Microbiol. 8:525-533.
37. Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
38. Tedin, K., A. Resch, M. Steiner, and U. Bläsi. 1995. Dual translational start motif evolutionarily conserved in the holin gene of Bacillus subtilis phage φ29. Virology 206:479-484.
39. Ton Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
40. Young, R. Unpublished data.
41. Young, R. 1992. Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56:430-481.
42. Young, R., and U. Bläsi. 1995. Holins: form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17:191-205.