We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The Bacteriophage T4 MotB Protein, a DNA-Binding Protein, Improves Phage Fitness.
- Authors
Patterson-West, Jennifer; Arroyo-Mendoza, Melissa; Hsieh, Meng-Lun; Harrison, Danielle; Walker, Morgan M.; Knipling, Leslie; Hinton, Deborah M.
- Abstract
The lytic bacteriophage T4 employs multiple phage-encoded early proteins to takeover the <italic>Escherichia coli</italic> host. However, the functions of many of these proteins are not known. In this study, we have characterized the T4 early gene <italic>motB</italic>, located in a dispensable region of the T4 genome. We show that heterologous production of MotB is highly toxic to <italic>E. coli</italic>, resulting in cell death or growth arrest depending on the strain and that the presence of <italic>motB</italic> increases T4 burst size 2-fold. Previous work suggested that <italic>motB</italic> affects middle gene expression, but our transcriptome analyses of T4 <italic>motBam</italic> vs. T4 wt infections reveal that only a few late genes are mildly impaired at 5 min post-infection, and expression of early and middle genes is unaffected. We find that MotB is a DNA-binding protein that binds both unmodified host and T4 modified [(glucosylated, hydroxymethylated-5 cytosine, (GHme-C)] DNA with no detectable sequence specificity. Interestingly, MotB copurifies with the host histone-like proteins, H-NS and StpA, either directly or through cobinding to DNA. We show that H-NS also binds modified T4 DNA and speculate that MotB may alter how H-NS interacts with T4 DNA, host DNA, or both, thereby improving the growth of the phage.
- Subjects
BACTERIOPHAGES; ESCHERICHIA coli; GENE expression; CARRIER proteins; CELL death
- Publication
Viruses (1999-4915), 2018, Vol 10, Issue 7, p343
- ISSN
1999-4915
- Publication type
Article
- DOI
10.3390/v10070343