scholarly journals Role of Escherichia coli Hfq in late-gene silencing of bacteriophage T4 dmd mutant

2002 ◽  
Vol 77 (5) ◽  
pp. 301-308 ◽  
Author(s):  
Hiroyuki Ueno ◽  
Tetsuro Yonesaki
Keyword(s):  
Escherichia Coli ◽  
Gene Silencing ◽  
Bacteriophage T4 ◽  
Late Gene

scholarly journals The Escherichia coli Inner Membrane Protein YhiM is Necessary for Efficient Attachment of Bacteriophage T4

Fine Focus ◽  
2018 ◽  
Vol 4 (1) ◽  
pp. 103-114
Author(s):  
M.A. Evans ◽  
P.T. Spieth ◽  
R.L. Sparks-Thissen
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Bacteriophage T4 ◽  
Inner Membrane ◽  
E Coli ◽  
Obligate Intracellular ◽  
Intracellular Parasites ◽  
Acid Shock ◽  
Inner Membrane Protein

Bacteriophages are obligate intracellular parasites, but many of the cellular proteins involved in replication have not been identified. We have tested the role of the inner membrane protein YhiM in bacteriophage replication. YhiM is a conserved (21) membrane protein in Escherichia coli (E. coli) thought to be localized to the cytoplasmic membrane that is necessary for cell survival under conditions of cell stress, including acid shock, low osmolarity and high temperature. We show here that YhiM is necessary for replication of the bacteriophage T4. It also plays a modest role in the replication of T1, T3, and T5 but it does not play a role in the replication of ΦX174. Our data indicated that no replication of T4 occurs in cells missing YhiM. This block in infection is due to a block in attachment of the virus to the cell surface.

scholarly journals The Central Spike Complex of Bacteriophage T4 Contacts PpiD in the Periplasm of Escherichia coli

Viruses ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 1135
Author(s):  
Sabrina Wenzel ◽  
Mikhail M. Shneider ◽  
Petr G. Leiman ◽  
Andreas Kuhn ◽  
Dorothee Kiefer
Keyword(s):  
Escherichia Coli ◽  
Cytoplasmic Membrane ◽  
Bacteriophage T4 ◽  
Infection Process ◽  
Host Cells ◽  
Phage Dna ◽  
Tail Structure ◽  
Contractile Tail ◽  
Periplasmic Chaperone

Infecting bacteriophage T4 uses a contractile tail structure to breach the envelope of the Escherichia coli host cell. During contraction, the tail tube headed with the “central spike complex” is thought to mechanically puncture the outer membrane. We show here that a purified tip fragment of the central spike complex interacts with periplasmic chaperone PpiD, which is anchored to the cytoplasmic membrane. PpiD may be involved in the penetration of the inner membrane by the T4 injection machinery, resulting in a DNA-conducting channel to translocate the phage DNA into the interior of the cell. Host cells with the ppiD gene deleted showed partial reduction in the plating efficiency of T4, suggesting a supporting role of PpiD to improve the efficiency of the infection process.

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