Involvement of a Bacterial Factor in Morphogenesis of Bacteriophage Capsid

Takano, Toshiya; Kakefuda, Tsuyoshi

doi:10.1038/newbio239034a0

Cited by 103 publications

(72 citation statements)

References 22 publications

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“…GroEL was identified in several laboratories in the 1970s as a bacterial protein required for phages T4 and lambda to replicate. Its precise role was unclear, but thought to involve the assembly of the phage head because rstb.royalsocietypublishing.org Phil Trans R Soc B 368: 20110398 a mutation in GroEL results in the head proteins forming an insoluble aggregate [16], but what its role in uninfected cells might be was not addressed. In 1988 it was also reported that antisera to GroEL identified a protein inside mitochondria from various plant and animal species [17].…”

Section: Generalizationmentioning

confidence: 99%

Assembly chaperones: a perspective

Ellis

2013

Phil. Trans. R. Soc. B

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The historical origins and current interpretation of the molecular chaperone concept are presented, with the emphasis on the distinction between folding chaperones and assembly chaperones. Definitions of some basic terms in this field are offered and misconceptions pointed out. Two examples of assembly chaperone are discussed in more detail: the role of numerous histone chaperones in fundamental nuclear processes and the co-operation of assembly chaperones with folding chaperones in the production of the world's most important enzyme.

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Section: Generalizationmentioning

confidence: 99%

Assembly chaperones: a perspective

Ellis

2013

Phil. Trans. R. Soc. B

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“…M ore than 30 years ago, the first genetic experiments were carried out that identified the groE operon of Escherichia coli as involved in macromolecular synthesis, observing it to be required for production of and T4 virus phage particles (1,2). Already in those first experiments it was recognized that groE mutations had effects on host cell growth in the absence of phage infection, implicating this operon in host cell metabolism.…”

mentioning

confidence: 99%

Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL

Chapman

Farr

Usaite

et al. 2006

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

134

171

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In a newly isolated temperature-sensitive lethal Escherichia coli mutant affecting the chaperonin GroEL, we observed wholesale aggregation of newly translated proteins. After temperature shift, transcription, translation, and growth slowed over two to three generations, accompanied by filamentation and accretion (in Ϸ2% of cells) of paracrystalline arrays containing mutant chaperonin complex. A biochemically isolated inclusion body fraction contained the collective of abundant proteins of the bacterial cytoplasm as determined by SDS͞PAGE and proteolysis͞MS analyses. Pulse-chase experiments revealed that newly made proteins, but not preexistent ones, were recruited to this insoluble fraction. Although aggregation of ''stringent'' GroEL͞GroES-dependent substrates may secondarily produce an ''avalanche'' of aggregation, the observations raise the possibility, supported by in vitro refolding experiments, that the widespread aggregation reflects that GroEL function supports the proper folding of a majority of newly translated polypeptides, not just the limited number indicated by interaction studies and in vitro experiments.chaperone ͉ misfolding ͉ protein folding

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“…The growth of phages might be prevented by the defect of maturation caused by the anomaly of the membrane. Several mutants of E. toll which suppressed the multiplication of phages T4 and lambda have been isolated so far (12)(13)(14)(15). The following results suggested that a single mutation affected both the cell division and phage multiplication in the case of E. toll strain ts612.…”

Section: Discussionmentioning

confidence: 80%

A Thermosensitive Mutant of Escherichia Coli With a Defect in the Process of Cell Division

Masamune

1975

J. Gen. Appl. Microbiol.

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A thermosensitive mutant of Escherichia coli (E. coli strain ts612) was isolated by the transduction of polA+ as a selective marker with phage Plc which had been mutagenized with hydroxylamine. The mutation was mapped between ilv (74.7 min) and metE (75.5 min). When the incubation temperature of this mutant was shifted from 30° to 42°, the cell division was interrupted immediately after the shift of temperature, although the optical density at 660 nm of the culture continued to increase for 90 min. The mutant did not support the multiplications of phages T4 and lambda at 42°, while it allowed the growth of phage T7. Electrophoretic analysis of membrane proteins of the mutant suggested that a part of the membrane protein was diminished when the mutant was incubated at the restrictive temperature.Specialized mutations in Escherichia coli can be induced by means of transduction with mutagenized phage P1. When an appropriate genetic marker was transduced with mutagenized phage particles, the transductants would involve a mutant which had a mutation closely linked to the selected marker. By this means it is possible to induce mutation in the specific region of the chromosome. Several mutants of Salmonella typhimurium were isolated by a similar method using a mutagenized phage P22 (1).With the intention of obtaining a new class of mutants having defects (2, 3) in the machinery of DNA synthesis, transduction of E. coli polA was made with the mutagenized phage Plc. Several thermosensitive mutants were isolated among the polA+ transductants and were characterized. Since one of these thermosensitive mutants seemed to have various interesting properties concerning the cell division and phage growth, the characterization of the mutant was performed which is described in this report.

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Involvement of a Bacterial Factor in Morphogenesis of Bacteriophage Capsid

Cited by 103 publications

References 22 publications

Assembly chaperones: a perspective

Assembly chaperones: a perspective

Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL

A Thermosensitive Mutant of Escherichia Coli With a Defect in the Process of Cell Division

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