The DOI matches its OpenAlex record; 94 of the 94 references it cites were found in a registry or an index.
Bacteriophage lysis: mechanism and regulation
Open accessAbstract
Bacteriophage lysis involves at least two fundamentally different strategies. Most phages elaborate at least two proteins, one of which is a murein hydrolase, or lysin, and the other is a membrane protein, which is given the designation holin in this review. The function of the holin is to create a lesion in the cytoplasmic membrane through which the murein hydrolase passes to gain access to the murein layer. This is necessary because phage-encoded lysins never have secretory signal sequences and are thus incapable of unassisted escape from the cytoplasm. The holins, whose prototype is the lambda S protein, share a common organization in terms of the arrangement of charged and hydrophobic residues, and they may all contain at least two transmembrane helical domains. The available evidence suggests that holins oligomerize to form nonspecific holes and that this hole-forming step is the regulated step in phage lysis. The correct scheduling of the lysis event is as much an essential feature of holin function as is the hole formation itself. In the second strategy of lysis, used by the small single-stranded DNA phage phi X174 and the single-stranded RNA phage MS2, no murein hydrolase activity is synthesized. Instead, there is a single species of small membrane protein, unlike the holins in primary structure, which somehow causes disruption of the envelope. These lysis proteins function by activation of cellular autolysins. A host locus is required for the lytic function of the phi X174 lysis gene E.
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Intervening Sequences of Regularly Spaced Prokaryotic Repeats Derive from Foreign Genetic Elements
Mojica, F. J. M., D�ez-Villase�or, C., Garc�a-Mart�nez, J., & Soria, E. (2005) · Journal of Molecular Evolution · doi:10.1007/s00239-004-0046-3 · Cited by 2,042
Explosive cell lysis as a mechanism for the biogenesis of bacterial membrane vesicles and biofilms
Turnbull, L., Toyofuku, M., Hynen, A. L., Kurosawa, M., Pessi, G., Petty, N. K., Osvath, S. R., Cárcamo-Oyarce, G., Gloag, E. S., Shimoni, R., et al. (2016) · Nature Communications · doi:10.1038/ncomms11220 · Cited by 709
Bacteriophage lysins as effective antibacterials
Fischetti, V. A. (2008) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.09.012 · Cited by 477
Molecular control of bacterial death and lysis
Rice, K. C., & Bayles, K. W. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00030-07 · Cited by 362
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Metadata
- Authors
- Young, R.
- Venue
- Microbiological Reviews
- Publisher
- American Society for Microbiology
- Published
- 1992-01-01
- Volume
- 56
- Issue
- 3
- Pages
- 430-481
- ISSN
- 0146-0749 (ISSN-L)
- OpenAlex
- W1852844868
- Cited by
- 773
- References
- 94
- FWCI
- 29.08
- Type
- journal article
- Language
- en
- Open access
- diamond
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