Targeting of GroEL to SecA on the cytoplasmic membrane of
            <i>Escherichia coli</i>

Bochkareva, Elena; Solovieva, Maria E.; Girshovich, A.S.

doi:10.1073/pnas.95.2.478

Cited by 50 publications

(31 citation statements)

References 45 publications

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“…We studied the lysis phenomenon of PRD1-infected groE mutant host cells, as the translocation and membrane insertion of holin proteins may be associated with chaperonin activity (5,13,22). E. coli strains carrying mutations in groEL or groES were tested for temperature sensitivity.…”

Section: Resultsmentioning

confidence: 99%

The Holin Protein of Bacteriophage PRD1 Forms a Pore for Small-Molecule and Endolysin Translocation

et al. 2005

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PRD1 is a bacteriophage with an icosahedral outer protein layer surrounding the viral membrane, which encloses the linear double-stranded DNA genome. PRD1 infects gram-negative cells harboring a conjugative IncP plasmid. Here we studied the lytic functions of PRD1. Using infected cells and plasmid-borne lysis genes, we demonstrated that a two-component lysis system (holin-endolysin) operates to release progeny phage particles from the host cell. Monitoring of ion fluxes and the ATP content of the infected cells allowed us to build a model of the sequence of lysis-related physiological changes. A decrease in the intracellular level of ATP is the earliest indicator of cell lysis, followed by the leakage of K ؉ from the cytosol approximately 20 min prior to the decrease in culture turbidity. However, the K ؉ efflux does not immediately lead to the depolarization of the cytoplasmic membrane or leakage of the intracellular ATP. These effects are observed only ϳ5 to 10 min prior to cell lysis. Similar results were obtained using cells expressing the holin and endolysin genes from plasmids.For most bacteriophages, host cell lysis requires, at a minimum, two proteins: an endolysin and a holin. Endolysins are small enzymes that degrade cell wall peptidoglycan. These enzymes fall into four groups depending on their activity, which is directed against the three different covalent linkages that maintain the integrity of the cell wall: (i) glycosylase and (ii) transglycosylase activities targeting the glycosidic linkages, and (iii) amidase and (iv) endopeptidase activities targeting the oligopeptide cross-linkages (39). Most endolysins characterized to date have no signal sequence and therefore accumulate in the cytosol during infection. Holins are small hydrophobic integral membrane proteins that permeabilize the cytoplasmic membrane (CM) and allow the endolysins to attack the peptidoglycan (20,38,39). In addition, holins may work as activators of the endolysins (39). Holins are grouped into two classes based on their primary structure. Class I holins, such as bacteriophage S protein, generally have more than 95 residues and form three transmembrane helices. Class II holins are smaller (65 to 95 residues) and form two transmembrane helices (18, 39).Holin-dependent lysis systems are highly regulated. The precise temporal regulation likely is dependent on the energy state of the CM, because adding a metabolic poison (e.g

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Section: Resultsmentioning

confidence: 99%

The Holin Protein of Bacteriophage PRD1 Forms a Pore for Small-Molecule and Endolysin Translocation

et al. 2005

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“…Furthermore, it was shown that GroEL interacts with SecA, and hence it was suggested that GroEL might be involved in the release of SecA from the membrane (22). Also, DnaK, DnaJ, and GrpE were shown to be involved in the export of a number of SecB-independent proteins, such as alkaline phosphatase, ␤-lactamase, and ribose-binding protein (327,328).…”

Section: Cytosolic Chaperonesmentioning

confidence: 99%

Signal Peptide-Dependent Protein Transport in Bacillus subtilis : a Genome-Based Survey of the Secretome

Tjalsma

Bolhuis

Jongbloed

et al. 2000

Microbiol Mol Biol Rev

751

768

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SUMMARY One of the most salient features of Bacillus subtilis and related bacilli is their natural capacity to secrete a variety of proteins into their environment, frequently to high concentrations. This has led to the commercial exploitation of bacilli as major “cell factories” for secreted enzymes. The recent sequencing of the genome of B. subtilis has provided major new impulse for analysis of the molecular mechanisms underlying protein secretion by this organism. Most importantly, the genome sequence has allowed predictions about the composition of the secretome, which includes both the pathways for protein transport and the secreted proteins. The present survey of the secretome describes four distinct pathways for protein export from the cytoplasm and approximately 300 proteins with the potential to be exported. By far the largest number of exported proteins are predicted to follow the major “Sec” pathway for protein secretion. In contrast, the twin-arginine translocation “Tat” pathway, a type IV prepilin-like export pathway for competence development, and ATP-binding cassette transporters can be regarded as “special-purpose” pathways, through which only a few proteins are transported. The properties of distinct classes of amino-terminal signal peptides, directing proteins into the various protein transport pathways, as well as the major components of each pathway are discussed. The predictions and comparisons in this review pinpoint important differences as well as similarities between protein transport systems in B. subtilis and other well-studied organisms, such as Escherichia coli and the yeast Saccharomyces cerevisiae. Thus, they may serve as a lead for future research and applications.

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“…A similar phenomenon was observed for another cytosolic molecular chaperone, trigger factor (TF) (18,44). In addition, some of these chaperones are also involved in the specific targeting of the preprotein to Sec translocation sites at the membrane (6,28).…”

Section: Vol 186 2004mentioning

confidence: 53%

A Little Help from My Friends: Quality Control of Presecretory Proteins in Bacteria

Fisher

DeLisa

2004

J Bacteriol

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Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coli

Cited by 50 publications

References 45 publications

The Holin Protein of Bacteriophage PRD1 Forms a Pore for Small-Molecule and Endolysin Translocation

The Holin Protein of Bacteriophage PRD1 Forms a Pore for Small-Molecule and Endolysin Translocation

Signal Peptide-Dependent Protein Transport in Bacillus subtilis : a Genome-Based Survey of the Secretome

A Little Help from My Friends: Quality Control of Presecretory Proteins in Bacteria

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