Peptide signal molecules and bacteriocins in Gram-negative bacteria: a genome-wide in silico screening for peptides containing a double-glycine leader sequence and their cognate transporters

Dirix, Gunter; Monsieurs, Pieter; Dombrecht, Bruno; Daniels, Ruth; Marchal, Kathleen; Vanderleyden, Jozef; Michiels, Jan

doi:10.1016/j.peptides.2003.10.028

Cited by 116 publications

(127 citation statements)

References 67 publications

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“…The precursors of these signaling peptides harbor a characteristic double-glycine leader that is removed concomitant with its export (184). A number of excellent reviews on this topic have been published (48,51,141,142,160,232,247). Therefore, we will concentrate our description on stimulus detection only.…”

Section: Regb/prrb-like Redox-responding Global Sensor Kinases With Smentioning

confidence: 99%

“…Activation of the corresponding TCS leads to a sudden burst in peptide release, thereby ensuring that the cells of a culture become activated at the same time to achieve synchronization. Examples include the development of competence for genetic transformation in the genera Bacillus (ComX-ComAP) and Streptococcus (ComC-ComDE), transition to the virulence state in Staphylococcus (AgrBCD), and bacteriocin production in various Firmicutes bacteria (48,51,141,142,160,232,247).…”

Section: Regb/prrb-like Redox-responding Global Sensor Kinases With Smentioning

confidence: 99%

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Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Mascher

Helmann

Unden

2006

Microbiol Mol Biol Rev

615

652

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SUMMARY Two-component signal-transducing systems are ubiquitously distributed communication interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental stimulus and a cognate response regulator that mediates the cellular response, mostly through differential expression of target genes. Histidine kinases are typically transmembrane proteins harboring at least two domains: an input (or sensor) domain and a cytoplasmic transmitter (or kinase) domain. They can be identified and classified by virtue of their conserved cytoplasmic kinase domains. In contrast, the sensor domains are highly variable, reflecting the plethora of different signals and modes of sensing. In order to gain insight into the mechanisms of stimulus perception by bacterial histidine kinases, we here survey sensor domain architecture and topology within the bacterial membrane, functional aspects related to this topology, and sequence and phylogenetic conservation. Based on these criteria, three groups of histidine kinases can be differentiated. (i) Periplasmic-sensing histidine kinases detect their stimuli (often small solutes) through an extracellular input domain. (ii) Histidine kinases with sensing mechanisms linked to the transmembrane regions detect stimuli (usually membrane-associated stimuli, such as ionic strength, osmolarity, turgor, or functional state of the cell envelope) via their membrane-spanning segments and sometimes via additional short extracellular loops. (iii) Cytoplasmic-sensing histidine kinases (either membrane anchored or soluble) detect cellular or diffusible signals reporting the metabolic or developmental state of the cell. This review provides an overview of mechanisms of stimulus perception for members of all three groups of bacterial signal-transducing histidine kinases.

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Section: Regb/prrb-like Redox-responding Global Sensor Kinases With Smentioning

confidence: 99%

Section: Regb/prrb-like Redox-responding Global Sensor Kinases With Smentioning

confidence: 99%

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Mascher

Helmann

Unden

2006

Microbiol Mol Biol Rev

615

652

View full text Add to dashboard Cite

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“…Originally generated in PDBSum (Laskowski, 2009). lysosomal pathway, while the C2 family members, the calciumdependent calpains, function in a variety of cellular processes such as signal transduction, apoptosis and cytoskeletal remodeling (Rawlings et al, 2012). The C39 endopeptidases are bacterial proteins responsible for the maturation of bacteriocin, a secreted bacterial antibiotic protein (Dirix et al, 2004). The catalytic activity of these enzymes is driven by a nucleophilic cysteine thiol and an electron-accepting histidine and often requires a third residue for the proper orientation of this cysteine-histidine pair.…”

Section: Gtge Is a Cysteine Proteasementioning

confidence: 99%

Structural and enzymatic characterization of a host-specificity determinant fromSalmonella

Kohler

Spanò

Galán

et al. 2014

Acta Crystallogr D Biol Crystallogr

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GtgE is an effector protein from Salmonella Typhimurium that modulates trafficking of the Salmonella-containing vacuole. It exerts its function by cleaving the Rab-family GTPases Rab29, Rab32 and Rab38, thereby preventing the delivery of antimicrobial factors to the bacteria-containing vacuole. Here, the crystal structure of GtgE at 1.65 Å resolution is presented, and structure-based mutagenesis and in vivo infection assays are used to identify its catalytic triad. A panel of cysteine protease inhibitors were examined and it was determined that N-ethylmaleimide, antipain and chymostatin inhibit GtgE activity in vitro. These findings provide the basis for the development of novel therapeutic strategies to combat Salmonella infections.

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“…Results from an in silico screening for peptides containing the double-glycine leader sequence and their cognate transporter have been published (25). The double-glycine leader motif that is found in a majority of class II and some class I bacteriocins and the unique N-terminal peptidase C39 domain of their cognate ABC transporters were the main features used in this search for such peptides (45,46).…”

Section: Peptide Bacteriocin Genes In Genome Sequencesmentioning

confidence: 99%