The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins

Cardarelli, Lia; Lam, Robert; Tuite, Ashleigh R.; Baker, Lindsay A.; Sadowski, Paul D.; Radford, Devon; Rubinstein, John L.; Battaile, Kevin P.; Chirgadze, Nickolay Y.; Maxwell, Karen L.; Davidson, Alan R.

doi:10.1016/j.jmb.2009.10.067

Cited by 70 publications

(73 citation statements)

References 62 publications

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“…This complementation reaction produced functional phage particles at a concentration of 10 9 pfu/mL. By contrast, a complementation reaction containing an HK97 74am lysate combined with an HK97 6am lysate, which contains normal tails with no functional DNA-filled heads (22), produced fewer than 100 pfu/mL. These complementation data show that HK97 74am phage produce normal active tails and no active heads, as might be expected if gp74 is required for terminase activity.…”

Section: Hk97 Gp74mentioning

confidence: 62%

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HNH proteins are a widespread component of phage DNA packaging machines

Kala

Cumby

Sadowski³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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120

106

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The genome packaging reactions of tailed bacteriophages and herpes viruses require the activity of a terminase enzyme, which is comprised of large and small subunits. Phage genomes are replicated as linear concatemers composed of multiple copies of the genome joined end to end. As the terminase enzyme packages the genome into the phage capsid, it cleaves the DNA into single genome-length units. In this work, we show that the phage HK97 HNH protein, gp74, is required for the specific endonuclease activity of HK97 terminase and is essential for phage head morphogenesis. HNH proteins are a very common family of proteins generally associated with nuclease activity that are found in all kingdoms of life. We show that the activity of gp74 in terminase-mediated cleavage of the phage cos site relies on the presence of an HNH motif active-site residue, and that the large subunit of HK97 terminase physically interacts with gp74. Bioinformatic analysis reveals that the role of HNH proteins in terminase function is widespread among long-tailed phages and is uniquely required for the activity of the Terminase_1 family of large terminase proteins.bacteriophage HK97 | HNH endonuclease | molecular chaperone

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Section: Hk97 Gp74mentioning

confidence: 62%

“…1D). gp13, the tail assembly chaperone of phage HK97, produces normal heads but no tails (24), and the 6am lysate contains empty heads that result from genome packaging and subsequent loss due to lack of the gp6 head-tail connector protein (22). They display dark internal staining and uniformly thin walls.…”

Section: Hk97 Gp74mentioning

confidence: 99%

HNH proteins are a widespread component of phage DNA packaging machines

Kala

Cumby

Sadowski³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

120

106

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“…Mutant capsids lacking the head completion proteins cannot bind tails and lose their DNA. In the Siphoviridae phages SPP1 and HK97, the ring closest to the portal is formed by dodecamers of gp15 (102 residues) 118 and gp6 (108 residues), 119 respectively. The SPP1_gp15 (Fig.…”

Section: 116mentioning

confidence: 99%

“…11A), and HK97. 118,119 The dodecamers, located below the portal vary significantly in size and shape. The P22 gp4 and the corresponding protein, gp11 from phage T7 (196-residues) form ring-like structures below the portal (Fig.…”

Section: Structure Of the Phage Tailsmentioning

confidence: 99%

Molecular architecture of tailed double-stranded DNA phages

2014

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“…The location of gp11 in the tail, together with its oligomerization change upon assembly (between monomer and dodecamer), strongly suggests that gp11 could be a gatekeeper protein that acts as an adaptor protein. In other phages these proteins also show a monomeric form that acquires a dodecameric architecture after interacting with the connector (3,13,37,38).…”

Section: Structure and Protein Composition Of The T7 Tail Complex-mentioning

confidence: 99%

Structural Characterization of the Bacteriophage T7 Tail Machinery

Cuervo¹,

Pulido-Cid²,

Chagoyen

et al. 2013

Journal of Biological Chemistry

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Background: T7 tail is involved in host recognition, DNA securing, and delivery. Results: The tail is formed by a tubular structure (proteins gp11 and gp12) surrounded by six fibers. Conclusion: gp11 is a gatekeeper-adaptor protein, and gp12 closes the ejection channel. Significance: Tailed bacteriophages may share a common molecular mechanism to coordinate the switch between DNA packaging and tail assembly.

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The Crystal Structure of Bacteriophage HK97 gp6: Defining a Large Family of Head–Tail Connector Proteins

Cited by 70 publications

References 62 publications

HNH proteins are a widespread component of phage DNA packaging machines

HNH proteins are a widespread component of phage DNA packaging machines

Molecular architecture of tailed double-stranded DNA phages

Structural Characterization of the Bacteriophage T7 Tail Machinery

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