Filnmentous phage assembly

Russel, Marjorie

doi:10.1111/j.1365-2958.1991.tb01907.x

Cited by 192 publications

(129 citation statements)

References 39 publications

(17 reference statements)

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“…GpI of filamentous bacteriophages is an integral membrane protein [7]. Comparison of the hydropathy plots for Zot and gp1 revealed considerable similarity, with one membrane-spanning segment located downstream from the putative NTPase domain being predicted for each protein (Fig.…”

Section: Zot Is a Membrane Proteinmentioning

confidence: 99%

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The second cholera toxin, Zot, and its plasmid‐encoded and phage‐encoded homologues constitute a group of putative ATPases with an altered purine NTP‐binding motif

Koonin

1992

FEBS Letters

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It is shown that the second cholera toxin, Zot, 0RF3 product of Pseudo~o/~s plasmid pKB740, and ORF424 product of bacteriophage Pfl arc a group of closely related proteins conlaining a modified version of the purinc NTP-binding motif, with a drastic substitution of tyrosinc for a conserved glycinc. They are distantly but reliably related to the product of gene I of filamentous bacteriophages which is a putative ATPase containing the classical NTP-binding motif and is involn;cd in iracteriophagc assembly and exit from the bacterial cell. Mydropathy analysis suggests that the Zot and gene I product may have a similar transmembtanc topology. It is hypothcsbecl thal Zot may possess ATPase activity and modify the membrane structure of its target cells in an ATP-dcpendcnt fashion. Genes for Zot and the related protein of pKB740 are likely to have evolved from gene 1 of a Pfl-like bacteriophage.

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Section: Zot Is a Membrane Proteinmentioning

confidence: 99%

“…In addition to its participation in phage assembly, gppl is involved in phage exit from the cell through induction of so-called contact zones betweec the inner and outer membranes [7]. When overexpressed, gp1 kills the bacterial eel1 through rapid loss of the membrane potential [13].…”

Section: Zot Is a Membrane Proteinmentioning

confidence: 99%

The second cholera toxin, Zot, and its plasmid‐encoded and phage‐encoded homologues constitute a group of putative ATPases with an altered purine NTP‐binding motif

Koonin

1992

FEBS Letters

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“…These results show that ATP hydrolysis is required for f1 assembly. Filamentous phage pI contains a well conserved Walker nucleotide binding motif (2), and a single amino acid change in the motif abolishes pI function (unpublished work). Hence it seems reasonable to propose that pI hydrolyzes ATP to catalyze assembly.…”

Section: Discussionmentioning

confidence: 99%

“…In the absence of functional thioredoxin, coat protein accumulates in the membrane, but particle extrusion from the cell does not occur (10). It has been suggested that thioredoxin promotes the processive replacement of pV by coat proteins, probably by an interaction with the cytoplasmic domain of pI (2).…”

mentioning

confidence: 99%

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A permeabilized cell system that assembles filamentous bacteriophage

Feng

Russel

Model

1997

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

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A permeabilized cell system has been developed that is capable of assembling filamentous phage only upon addition of exogenous thioredoxin. The in vitro system exhibits the same component requirements seen in vivo: functional thioredoxin, an intact packaging signal in the substrate DNA, and the assembly protein, pIV. This crude in vitro system is insensitive to inhibitors of protein or DNA synthesis, demonstrating that particle assembly uses components that had accumulated before cell permeabilization. The temporal separation of the synthetic period, during which phage proteins and DNA accumulate, from the assembly period enabled us to examine the energy requirement for assembly. We show here that ATP hydrolysis is required for filamentous phage assembly and that the proton motive force is also important.

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Bacteriophages and biotechnology: a review

Marks

Sharp

2000

J. Chem. Technol. Biotechnol.

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Bacteriophages are viruses whose hosts are bacterial cells. Like all viruses, phages are metabolically inert in their extra-cellular form, reproducing only after infecting suitable host bacteria. Discovered over 80 years ago, they have played a key role in the development of modern biotechnology. Their initial isolation appeared to offer the ®rst therapeutic for the control of infectious disease. The discovery of antibiotics in the 1940s eclipsed bacteriophage-based therapies although, with the increase in multiply drug-resistant pathogens, bacteriophages are being re-evaluated as the basis of new therapeutic strategies. Their de®ned host speci®city facilitated their application in the typing and identi®cation of a wide range of bacteria. Bacteriophage typing schemes were developed for most groups of pathogenic of bacteria and more recently their host speci®city has been applied to the development of bacterial detection and diagnostic strategies. The advance in molecular biology over the past 30 years has been built on the study of phage structure and genetics carried out through the 1950s and 1960s. Restriction endonucleases which form the basis of molecular cloning were developed following studies of phage infection and many phage enzymes provide tools for the molecular biologist. The technique of phage display has more recently provided a powerful technique for the identi®cation and optimisation of ligands for antibodies and other biomolecules. In the environment they have been widely applied as tracers, as indicators of pollution and in the monitoring and validation of biological ®lters. While providing a valuable resource to the development of modern biotechnology, their ability to mobilise and transfer toxin genes in the environment is viewed with concern. They also present a continuing challenge to the fermentation and in particular, the dairy industry, where phage infection can prove commercially disastrous.

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Filnmentous phage assembly

Cited by 192 publications

References 39 publications

The second cholera toxin, Zot, and its plasmid‐encoded and phage‐encoded homologues constitute a group of putative ATPases with an altered purine NTP‐binding motif

The second cholera toxin, Zot, and its plasmid‐encoded and phage‐encoded homologues constitute a group of putative ATPases with an altered purine NTP‐binding motif

A permeabilized cell system that assembles filamentous bacteriophage

Bacteriophages and biotechnology: a review

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