PMID:10931329

Citation	Moak, M and Molineux, IJ (2000) Role of the Gp16 lytic transglycosylase motif in bacteriophage T7 virions at the initiation of infection. Mol. Microbiol. 37:345-55
Abstract	The predicted catalytic glutamate residue for transglycosylase activity of bacteriophage T7 gp16 is not essential for phage growth, but is shown to be beneficial during infection of Escherichia coli cells grown to high cell density, conditions in which murein is more highly cross-linked. In the absence of the putative transglycosylase, internalization of the phage genome is significantly delayed during infection. The lytic transglycosylase motif of gp16 is essential for phage growth at temperatures below 20 degrees C, indicating that these growth conditions also lead to increased cross-linking of peptidoglycan. Overexpression of sltY, E. coli soluble lytic transglycosylase, partially complements the defect in infection of mutant phage particles, allowing them to infect at higher efficiencies. Conversely, an sltY deletion increases the latent period of wild-type phage.
Links	PubMed
Keywords	Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage T7/enzymology; Bacteriophage T7/growth & development; Bacteriophage T7/pathogenicity; Escherichia coli/metabolism; Escherichia coli/virology; Escherichia coli Proteins; Glutamic Acid/genetics; Glycoside Hydrolases; Glycosyltransferases/chemistry; Glycosyltransferases/genetics; Glycosyltransferases/metabolism; Lysogeny; Molecular Sequence Data; Peptidoglycan/metabolism; Sequence Homology, Amino Acid; Viral Core Proteins/chemistry; Viral Core Proteins/genetics; Viral Core Proteins/metabolism; Virion/enzymology; Virion/growth & development; Virion/pathogenicity; Virulence
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Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status

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