scholarly journals The lysis cassette of DLP12 defective prophage is regulated by RpoE

Microbiology ◽  
2015 ◽  
Vol 161 (8) ◽  
pp. 1683-1693 ◽  
Author(s):  
Karl-Gustav Rueggeberg ◽  
Faustino A. Toba ◽  
Jeremy G. Bird ◽  
Nathan Franck ◽  
Mitchell G. Thompson ◽  
...  
1971 ◽  
Vol 18 (1) ◽  
pp. 9-19 ◽  
Author(s):  
R. W. Hedges

SUMMARYBacteriophageεγis capable of transduction both by replacement of a genetic segment of the recipient by the homologous genetic material from the donor strain and by the formation of defective transducing particles capable of lysogenizing the recipient strain ofS. anatum.The isolation of strains carrying such prophages, which have incorporated the lactose or arabinose operons, is reported. Lysogenic strains, carrying both normal and defective transducing prophage, form high-frequency transducing lysates. Other strains, carrying only defective prophage, show evidence that the association of prophage genes and transduced materials is stable since the loss of one frequently entails loss of the other.


2019 ◽  
Vol 8 (18) ◽  
Author(s):  
Chandler O’Leary ◽  
Yicheng Xie ◽  
Rohit Kongari ◽  
Jason J. Gill ◽  
Mei Liu

Bacteriophage Siskin is a member of the χ-like siphovirus phage cluster that infects Salmonella enterica serovar Typhimurium strain LT2. Here, we report the complete 58,476-bp sequence of the Siskin genome, provide confirmation of its genomic termini, and describe a potentially new class of holins and endolysins found in the lysis cassette.


2013 ◽  
Vol 42 (4) ◽  
pp. 2725-2735 ◽  
Author(s):  
Ronnie P.-A. Berntsson ◽  
Richard Odegrip ◽  
Wilhelmina Sehlén ◽  
Karin Skaar ◽  
Linda M. Svensson ◽  
...  

Abstract The Cox protein from bacteriophage P2 is a small multifunctional DNA-binding protein. It is involved in site-specific recombination leading to P2 prophage excision and functions as a transcriptional repressor of the P2 Pc promoter. Furthermore, it transcriptionally activates the unrelated, defective prophage P4 that depends on phage P2 late gene products for lytic growth. In this article, we have investigated the structural determinants to understand how P2 Cox performs these different functions. We have solved the structure of P2 Cox to 2.4 Å resolution. Interestingly, P2 Cox crystallized in a continuous oligomeric spiral with its DNA-binding helix and wing positioned outwards. The extended C-terminal part of P2 Cox is largely responsible for the oligomerization in the structure. The spacing between the repeating DNA-binding elements along the helical P2 Cox filament is consistent with DNA binding along the filament. Functional analyses of alanine mutants in P2 Cox argue for the importance of key residues for protein function. We here present the first structure from the Cox protein family and, together with previous biochemical observations, propose that P2 Cox achieves its various functions by specific binding of DNA while wrapping the DNA around its helical oligomer.


2004 ◽  
Vol 233 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Steve Labrie ◽  
NataÅ¡a Vukov ◽  
Martin J Loessner ◽  
Sylvain Moineau

PLoS ONE ◽  
2015 ◽  
Vol 10 (11) ◽  
pp. e0142504 ◽  
Author(s):  
Jung Seok Lee ◽  
Ho Bin Jang ◽  
Ki Sei Kim ◽  
Tae Hwan Kim ◽  
Se Pyeong Im ◽  
...  

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_4) ◽  
pp. 691-700 ◽  
Author(s):  
Karl-Gustav Rueggeberg ◽  
Faustino A. Toba ◽  
Mitchell G. Thompson ◽  
Bryan R. Campbell ◽  
Anthony G. Hay

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