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PMID:18348984

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Citation

Boulanger, P, Jacquot, P, Plançon, L, Chami, M, Engel, A, Parquet, C, Herbeuval, C and Letellier, L (2008) Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities. J. Biol. Chem. 283:13556-64

Abstract

We report a bioinformatic and functional characterization of Pb2, a 121-kDa multimeric protein that forms phage T5 straight fiber and is implicated in DNA transfer into the host. Pb2 was predicted to consist of three domains. Region I (residues 1-1030) was mainly organized in coiled coil and shared features of tape measure proteins. Region II (residues 1030-1076) contained two alpha-helical transmembrane segments. Region III (residues 1135-1148) included a metallopeptidase motif. A truncated version of Pb2 (Pb2-Cterm, residues 964-1148) was expressed and purified. Pb2-Cterm shared common features with fusogenic membrane polypeptides. It formed oligomeric structures and inserted into liposomes triggering their fusion. Pb2-Cterm caused beta-galactosidase release from Escherichia coli cells and in vitro peptidoglycan hydrolysis. Based on these multifunctional properties, we propose that binding of phage T5 to its receptor triggers large conformational changes in Pb2. The coiled coil region would serve as a sensor for triggering the opening of the head-tail connector. The C-terminal region would gain access to the host envelope, permitting the local degradation of the peptidoglycan and the formation of the DNA pore by fusion of the two membranes.

Links

PubMed Online version:10.1074/jbc.M800052200

Keywords

Amino Acid Sequence; Bacteriophages/chemistry; Computational Biology/methods; DNA, Viral/chemistry; Hydrolysis; Microscopy, Electron; Molecular Sequence Data; Peptides/chemistry; Polysaccharides/chemistry; Protein Conformation; Protein Structure, Tertiary; Sucrose/chemistry; Time Factors; Viral Proteins/chemistry; Viral Tail Proteins/chemistry; Viral Tail Proteins/physiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

BPT5:TMP

involved_in

GO:0044409: entry into host

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

BPT5:TTTP

Contributes to

GO:0098015: virus tail

ECO:0000247:

PMID:17056065[1]


C

Using bioinformatic analysis, p142 was aligned with the gpU tail-terminator protein from bacteriophage lambda. Due to it's similarity, p142 was determined to be a putative tail terminator.

complete
CACAO 12025

BPT5:TMP

GO:0061783: peptidoglycan muralytic activity

ECO:0000314:

F

According to the paper the protein specifically the C terminus end is involved in the degradation of peptidoglycan . The protein has peptidoglycan hydrolase activity. When mixed with peptidoglycan it was shown to give products and degrade peptidoglycan using it as a substrate. Figure six shows the hydrolytic capability of the protein by comparing it to sonicated ( sonication is a method used to disrupt cell membranes) cells. With the PB2-Cterm we can see that the B galactosidase coming out from the bacteria reached a level 60 percent to that of sonicated cells. Which is further proof of peptidoglycan hyrolysis. The control designed for this part was only adding DDM which didn't end up causing any B galactosidase to come out of the bacteria.

complete
CACAO 13184

BPT5:TMP

involved_in

GO:0098003: viral tail assembly

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

BPT5:TMP

involved_in

GO:0085027: entry into host via enzymatic degradation of host anatomical structure

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

Notes

See also

References

See Help:References for how to manage references in GONUTS.

  1. Edmonds, L et al. (2007) The NMR structure of the gpU tail-terminator protein from bacteriophage lambda: identification of sites contributing to Mg(II)-mediated oligomerization and biological function. J. Mol. Biol. 365 175-86 PubMed GONUTS page