Escherichia coli SecB, SecA, and SecY proteins are required for expression and membrane insertion of the bacteriocin release protein, a small lipoprotein

Oudega, Bauke; Mol, Olaf; Ulsen, Peter van; Stegehuis, Freek; Wal, F.J. van der; Luirink, Joen

doi:10.1128/jb.175.5.1543-1547.1993

Cited by 8 publications

(6 citation statements)

References 40 publications

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“…However, the rate of its synthesis is particularly slow, allowing the detection of all intermediate forms at any given time in the producing cells (6). A similar slow rate of synthesis has been observed for another lysis protein, the cloacin DF13 release protein (16). This rate of synthesis is unique among exported proteins, and its cause is unknown.…”

mentioning

confidence: 78%

Effects of temperature and of heat shock on the expression and action of the colicin A lysis protein

Cavard

1995

J Bacteriol

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At low temperature, the synthesis of the colicin A lysis protein in Escherichia coli was slowed down, and consequently its functioning was retarded. The rates were restored when the bacteria were shifted for 10 min to 42؇C, except in an rpoH mutant, suggesting that one or more proteins regulated by 32 is necessary for expression of colicin A lysis protein.The colicin A lysis protein, called Cal, is a lipopeptide responsible for the export of colicin A by Escherichia coli carrying plasmid pColA. Its synthesis is performed in various steps, like that of all bacterial lipoproteins (11). However, the rate of its synthesis is particularly slow, allowing the detection of all intermediate forms at any given time in the producing cells (6). A similar slow rate of synthesis has been observed for another lysis protein, the cloacin DF13 release protein (16). This rate of synthesis is unique among exported proteins, and its cause is unknown. The simultaneous presence of precursor and mature forms of exported proteins is usually obtained by drastic means such as gene mutations or use of drugs, which affect significantly the life of the cell. It provokes the induction of the heat shock response (20). Previous experiments have suggested that Cal mimics the consequences of growth at elevated temperatures and elicits the same responses (7). The fact that the synthesis of Cal occurs similarly at 42ЊC as at 37ЊC (3) might indicate that Cal induces the heat shock regulon at the normal temperature. To verify this, the functioning and synthesis of Cal were successively studied at both low and high temperatures. Surprisingly, they were modified at low but not at high temperature.Quasi-lysis is delayed at low temperature. Quasi-lysis corresponds to a gentle decline in the turbidity of the culture occurring 1 to 2 h after induction of every colicin lysis protein (reviewed in reference 8). The effect of temperature was checked on quasi-lysis provoked by Cal on cells carrying either plasmid pColA9, which contains the wild-type colicin A operon (14), or plasmid pCK4, which contains the cal gene under the tac promoter (6) (Fig. 1). W3110/pColA9 cells grown at 30ЊC were induced for colicin A and Cal synthesis and incubated at either 30, 37, or 42ЊC. At each temperature, the turbidity first increased with time along with the control cells and decreased some time afterward. Both the timing and the rate of the decline in the culture turbidity differed according to the temperature of incubation. The decrease began after 1 h of induction at either 42 or 37ЊC but only after 3 h at 30ЊC. The rate of decline in the culture turbidity was fast at 42ЊC, a little less rapid at 37ЊC, and particularly slow at 30ЊC. It seemed that Cal did not stop the growth of the cells at 30ЊC as efficiently as it did at either 37 or 42ЊC. Similar, although less significant, results were obtained for induced W3110/pCK4 cells.The experiments were repeated with cells with a missense mutation in the pldA gene, which encodes the phospholipase A of the outer membrane (2), as ...

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confidence: 78%

Effects of temperature and of heat shock on the expression and action of the colicin A lysis protein

Cavard

1995

J Bacteriol

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“…The signal peptides of Cal, CelB (colicin E2 lysis protein), and BRP are stable after cleavage and accumulate in the inner membrane, while that of CelA is immediately degraded (80a, 84, 91, 99, 424, 425, 539). The dependence on the Sec machinery also varies from one lysis protein to another: CelA and BRP are Sec dependent, while Cal is Sec independent (81,499).…”

Section: Sequence Synthesis and Localization Of The Colicin Lysis Pmentioning

confidence: 99%

Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

985

1,324

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SUMMARY Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

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“…The colicin El-and pCloDFI3 BRP strongly depend on SecA and SecY for their translocation across the cytoplasmic membrane [106,107], as does Lpp [108,109]. However, the colicin A BRP appeared to be less dependent on SecA and SecY, since this BRP was found to be slowly processed in secA and secY mutants [106].…”

Section: Lipid Modification Processing and Subcellular Localizationmentioning

confidence: 96%

“…However, the colicin A BRP appeared to be less dependent on SecA and SecY, since this BRP was found to be slowly processed in secA and secY mutants [106]. Furthermore, it was shown that transiocation of the pCIoDFI3 BRP depends on SecB [107], in contrast to Lpp [108,109]. The high similarity of the primary structures of the mature [72,88,99,114].…”

Section: Lipid Modification Processing and Subcellular Localizationmentioning

confidence: 98%

Bacteriocin release proteins: mode of action, structure, and biotechnological application

Wal

Luirink

Oudega

1995

FEMS Microbiology Reviews

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The mechanism by which Gram-negative bacteria like Escherichia coli secrete bacteriocins into the culture medium is unique and quite different from the mechanism by which other proteins are translocated across the two bacterial membranes, namely through the known branches of the general secretory pathway. The release of bacteriocins requires the expression and activity of a so-called bacteriocin release protein and the presence of the detergent-resistant phospholipase A in the outer membrane. The bacteriocin release proteins are highly expressed small lipoproteins which are synthesized with a signal peptide that remains stable and which accumulates in the cytoplasmic membrane after cleavage. The combined action of these stable, accumulated signal peptides, the lipid-modified mature bacteriocin release proteins (BRPs) and phospholipase A cause the release of bacteriocins. The structure and mode of action of these BRPs as well as their application in the release of heterologous proteins by E. coli is described in this review.

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Escherichia coli SecB, SecA, and SecY proteins are required for expression and membrane insertion of the bacteriocin release protein, a small lipoprotein

Cited by 8 publications

References 40 publications

Effects of temperature and of heat shock on the expression and action of the colicin A lysis protein

Effects of temperature and of heat shock on the expression and action of the colicin A lysis protein

Colicin Biology

Bacteriocin release proteins: mode of action, structure, and biotechnological application

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