Signal Recognition Particle (SRP)-mediated Targeting and Sec-dependent Translocation of an Extracellular Escherichia coli Protein

Sijbrandi, Robert; Urbanus, Malene L.; Hagen-Jongman, Corinne M. ten; Bernstein, Harris; Oudega, Bauke; Otto, Ben R.; Luirink, Joen

doi:10.1074/jbc.m211630200

Cited by 108 publications

(110 citation statements)

References 30 publications

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“…7) further supports the involvement of FlhF in the regulation of protein secretion, as already reported for P. putida (Pandza et al, 2000). FlhF is a member of the SRP-GTPase family (Carpenter et al, 1992;Pandza et al, 2000) and shows substantial homology with Ffh and FtsY, two proteins required for extracellular accumulation of proteins in E. coli and B. subtilis (Sijbrandi et al, 2003;Zanen et al, 2006). Similarly to flhF disruption in B. cereus, Ffh or FtsY depletion in B. subtilis determines an increased level of various extracellular proteins (Zanen et al, 2006).…”

Section: Discussionmentioning

confidence: 53%

FlhF, a signal recognition particle-like GTPase, is involved in the regulation of flagellar arrangement, motility behaviour and protein secretion in Bacillus cereus

et al. 2007

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Section: Discussionmentioning

confidence: 53%

FlhF, a signal recognition particle-like GTPase, is involved in the regulation of flagellar arrangement, motility behaviour and protein secretion in Bacillus cereus

et al. 2007

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“…These signal peptides contain a ϳ25-amino acid segment that resembles typical signal peptides as well as a ϳ25-amino acid N-terminal extension of unknown function. Previous results indicate that one member of the SPATE family, Hbp, is targeted to the IM by SRP (34). To determine whether the basic residues found in SPATE signal peptides promote SRP recognition, we first replaced the native signal peptides of MBP and OmpA, two proteins that are normally targeted by SecB, with either the complete EspP signal peptide or a truncated version that lacks the N-terminal extension (⌬Esp).…”

Section: Resultsmentioning

confidence: 99%

Basic Amino Acids in a Distinct Subset of Signal Peptides Promote Interaction with the Signal Recognition Particle

Peterson

Woolhead

Bernstein

2003

Journal of Biological Chemistry

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Previous studies have demonstrated that signal peptides bind to the signal recognition particle (SRP) primarily via hydrophobic interactions with the 54-kDa protein subunit. The crystal structure of the conserved SRP ribonucleoprotein core, however, raised the surprising possibility that electrostatic interactions between basic amino acids in signal peptides and the phosphate backbone of SRP RNA may also play a role in signal sequence recognition. To test this possibility we examined the degree to which basic amino acids in a signal peptide influence the targeting of two Escherichia coli proteins, maltose binding protein and OmpA. Whereas both proteins are normally targeted to the inner membrane by SecB, we found that replacement of their native signal peptides with another moderately hydrophobic but unusually basic signal peptide (⌬EspP) rerouted them into the SRP pathway. Reduction in either the net positive charge or the hydrophobicity of the ⌬EspP signal peptide decreased the effectiveness of SRP recognition. A high degree of hydrophobicity, however, compensated for the loss of basic residues and restored SRP binding. Taken together, the data suggest that the formation of salt bridges between SRP RNA and basic amino acids facilitates the binding of a distinct subset of signal peptides whose hydrophobicity falls slightly below a threshold level.

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“…Recently, two papers have been published that could give some clues. In these papers, Sijbrandi et al (12) and Szabady et al (13) study another group of large outer membrane proteins, the autotransporters. A subset of autotransporters also contains unusually long signal sequences that are, in fact, similar in composition to those of the TonB-dependent transducers (Fig.…”

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confidence: 99%

“…1). Sijbrandi et al (12) showed that these long signal sequences interact with the Sec translocon and with the signal recognition particle. This means that these proteins are transported cotranslationally.…”

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confidence: 99%

Iron Gate: the Translocation System

Llamas

Bitter

2006

J Bacteriol

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Siderophores have been studied in great detail over the last 20 years, and although our knowledge of these special iron carriers is vast, new insights and new twists to this well-told story are regularly appearing. In this issue of Journal of Bacteriology, Voulhoux et al. (15) describe the effect of the twinarginine translocation (Tat) system on the biosynthesis and the uptake of siderophores by Pseudomonas aeruginosa. The Tat pathway is a specialized transport system for the translocation of folded proteins across the cytoplasmic membrane. The signal sequences of proteins that are translocated via the Tat pathway almost invariantly possess a twin-arginine (RR) motif and are usually longer than Sec secretion signal peptides. So, is it not possible to predict all Tat substrates from the primary sequence of the signal sequence? The article of Voulhoux et al. shows that this is not the case, and the reason is that some signal sequences just do not seem to obey the general rules. An example is the FpvA siderophore receptor of P. aeruginosa.Siderophores are low-molecular-weight catechol or hydroxamate compounds that bind iron with high affinity and are therefore able to sequester and solubilize minute quantities of free iron present in the environment. These secreted iron scavengers have to be recaptured by the bacterium. For this, gramnegative bacteria have developed a special outer membrane transport system that consists of a dedicated outer membrane receptor and a cytoplasmic membrane complex composed of the ExbB, ExbD, and TonB proteins. The TonB system transduces the proton-motive force of the cytoplasmic membrane to the high-affinity outer membrane receptors, which are therefore known as TonB-dependent receptors. Siderophore-mediated scavenging of iron is a sufficient and widespread mechanism, but there is, however, a more favorable alternative: why waist energy on the production of siderophores that are secreted and might never return, if you could also steal them from your neighbors? In fact, that is exactly what happens. Some bacteria produce a large array of different TonB-dependent receptors, each with its own specificity, in order to steal their neighbors' siderophores (heterologous siderophores) loaded with iron. The human opportunistic pathogen P. aeruginosa, for instance, possesses receptors for its own siderophores pyoverdine and pyochelin, but in addition it has the ability to produce 32 other TonB-dependent receptors. These additional receptors are used for the uptake of enterobactin produced by different Enterobacteriaceae (4, 6) and ferrioxamine or ferrichrome produced by several bacteria and fungi, respectively (9). The beauty of many of these receptors is that they are produced normally in tiny amounts and are induced only upon

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Signal Recognition Particle (SRP)-mediated Targeting and Sec-dependent Translocation of an Extracellular Escherichia coli Protein

Cited by 108 publications

References 30 publications

FlhF, a signal recognition particle-like GTPase, is involved in the regulation of flagellar arrangement, motility behaviour and protein secretion in Bacillus cereus

FlhF, a signal recognition particle-like GTPase, is involved in the regulation of flagellar arrangement, motility behaviour and protein secretion in Bacillus cereus

Basic Amino Acids in a Distinct Subset of Signal Peptides Promote Interaction with the Signal Recognition Particle

Iron Gate: the Translocation System

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