The λ holin accumulates beyond the lethal triggering concentration under hyperexpression conditions

Gene Expression

Volumn 7, Issue 1, 1998, Pages 39-52

  Smith, David L ^a   Chang, Chung Yu ^a,b   Young, R Y ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b NONE   (United States)

Author keywords

Bacteriophage lysis; Holin; Overexpression

Indexed keywords

MEMBRANE PROTEIN; OLIGONUCLEOTIDE; VITRONECTIN;

ARTICLE; BACTERIOPHAGE LAMBDA; CYTOLYSIS; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE EXPRESSION SYSTEM; GENE INDUCTION; GENE OVEREXPRESSION; MOLECULAR CLONING; NONHUMAN; PLASMID;

BACTERIOPHAGE LAMBDA; ESCHERICHIA COLI; UNIDENTIFIED BACTERIOPHAGE;

EID: 0031923724     PISSN: 10522166     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (33)

1. Bläsi, U.; Chang, C.-Y.; Zagotta, M. T.; Nam, K.; Young, R. The lethal lambda S gene encodes its own inhibitor. EMBO J. 9:981-989; 1990.
2. Bläsi, U.; Nam, K.; Hartz, D.; Gold, L.; Young, R. Dual translational initiation sites control function of the lambda S gene. EMBO J. 8:3501-3510; 1989.
3. Bläsi, U., Young, R. Two beginnings for a single purpose: The dual-start holins in the regulation of phage lysis. Mol. Microbiol. 21:675-682; 1996.
4. Casjens, S.; Eppler, K.; Parr, R.; Poteete, A. R. Nucleotide sequence of the bacteriophage P22 gene 19 to 3 region: Identification of a new gene required for lysis. Virology 171(2):588-598; 1989.
5. Chang C-Y. Synthesis, function and regulation of the lambda holin. Ph.D. dissertation; 1994.
6. Chang, C.-Y.; Nam, K.; Young, R. S gene expression and the timing of lysis by bacteriophage lambda. J. Bacteriol. 177:3283-3294; 1995.
7. Chung, C. T.; Niemela, S. L.; Miller, R. H. One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA 86: 2172-2175; 1989.
8. Fischer, B.; Sumner, I.; Goodenough, P. Isolation and renaturation of bio-active proteins expressed in Escherichia coli as inclusion bodies. Arzneimittelforschung 42:1512-1515; 1992.
9. Pürste, J. P.; Pansegrau, W.; Frank, R.; Blöcker, H.; Scholz, P.; Bagdasarian, M.; Lanka, E. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48: 119-131; 1986.
10. Garrett, J.; Bruno, C.; Young, R. Lysis protein S of phage lambda functions in Saccharomyces cerevisiae. J. Bacteriol. 172:7275-7277; 1990.
11. Garrett, J.; Fusselman, R.; Hise, J.; Chiou, L.; Smith-Grillo, D.; Schulz, R.; Young, R. Cell lysis by induction of cloned lambda lysis genes. Mol. Gen. Genet. 182:326-331; 1981.
12. 0 ATP synthase in Escherichia coli: Gln-252 through Tyr-263. J. Bacteriol. 175:1337-1343; 1993.
13. Johnson-Boaz, R.; Chang, C.-Y.; Young, R. A dominant mutation in the bacteriophage lambda S gene causes premature lysis and an absolute defective plating phenotype. Mol. Microbiol. 13:495-504; 1994.
14. Miller, J. H. A short course in bacterial genetics: A laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1992.
15. 0 ATPase. J. Bacteriol. 176:1383-1389; 1994.
16. Nam K. Translational regulation of the S gene of bacteriophage lambda. Ph.D. dissertation; 1991.
17. Osborn, M. J.; Gander, J. E.; Parisi, E. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Site of synthesis of lipopolysaccharide. J. Biol. Chem. 247:3973-3986; 1972.
18. Raab, R.; Neal, G.; Garrett, J.; Grimaila, R.; Fusselman, R.; Young, R. Mutational analysis of bacteriophage lambda lysis gene S. J. Bacteriol. 167: 1035-1042; 1986.
19. Raab, R.; Neal, G.; Sohaskey, C.; Smith, J.; Young, R. Dominance in lambda S mutations and evidence for translational control. J. Mol. Biol. 199:95-105; 1988.
20. Rennell, D.; Poteete, A. R. Phage P22 lysis genes: Nucleotide sequences and functional relationships with T4 and lambda genes. Virology 143:280-289; 1985.
21. Rosenberg, A. H.; Lade, B. N.; Chui, D.-S.; Lin, S.-W.; Dunn, J. J.; Studier, F. W. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene 56:125-135; 1987.
22. Sambrook, J.; Fritsch, E. F.; Maniatis, T. Molecular cloning: A laboratory manual, 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Press; 1989.
23. Schägger, H.; von Jagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379; 1987.
24. Schnaitman, C. A. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J. Bacteriol. 108:545-552; 1971.
25. Silhavy, T. J.; Berman, M. L.; Enquist, L. W. Bacterial strains. In: Silhavy, T. J.; Berman, M. L.; Enquist, L. W., eds. Experiments with gene fusions. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; 1984:xi-xiii.
26. Singh, A. P.; Bragg, P. D. ATP-dependent proton translocation and quenching of 9-amino acridine fluorescence in inside-out membrane vesicles of a cytochrome-deficient mutant of Escherichia coli. Biochim. Biophys. Acta 464:562-570; 1977.
27. Steiner, M.; Bläsi, U. Charged amino-terminal amino acids affect the lethal capacity of lambda lysis proteins S107 and S105. Mol. Microbiol. 8: 525-533; 1993.
28. Studier, F. W.; Moffatt, B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189: 113-130; 1986.
29. Towbin, H.; Staehelin, T.; Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354; 1979.
30. Wessel, D.; Flügge, U. I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138:141-143; 1984.
31. Young, R.; Bläsi, U. Holins: Form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17:191-205; 1995.
32. Young, R.; Way, S.; Yin, J.; Syvanen, M. Transposition mutagenesis of bacteriophage lambda: A new gene affecting cell lysis. J. Mol. Biol. 132:307-322; 1979.
33. Zagotta, M. T.; Wilson, D. B. Oligomerization of the bacteriophage lambda S protein in the inner membrane of E. coli. J. Bacteriol. 172:912-921; 1990.