An extracellular factor regulating expression of the chromosomal aminoglycoside 2'-N-acetyltransferase of Providencia stuartii

Rather, Philip N.; Parojcic, Milica M.; Paradise, Michael R.

doi:10.1128/aac.41.8.1749

Cited by 35 publications

(16 citation statements)

References 45 publications

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“…This mutant contained a single Tn917 insertion and was stable after repeated subculturing in selective media. The phenotype of this mutant suggested that a key gene involved in transcription, translation, or posttranslation regulation, similar to those previously identified in S. aureus and other organisms (1,9,23,38,40,49,50), was mutated.…”

supporting

confidence: 72%

Identification of pel , a Streptococcus pyogenes Locus That Affects both Surface and Secreted Proteins

Sledjeski

Kreikemeyer

et al. 1999

J Bacteriol

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A Tn917 insertion mutant of an M49 serotype, opacity factor-positive Streptococcus pyogenes, was isolated. It had the following phenotypes: decreased β-hemolysis mediated by streptolysin S, reduction in the activity of a secreted cysteine protease and streptokinase, and an altered immunoglobulin and fibrinogen-binding phenotype. The site of insertion of Tn917 into the chromosome and the surrounding sequence, thepel region (pleiotropic effect locus), was determined. Phage A25 transduction confirmed that the pleiotropic changes in phenotype could be cotransduced with Tn917. Thepel region was cloned and sequenced, and the transposon was found to be inserted upstream of a single open reading frame which led to a failure to transcribe a 500-base mRNA. The loss of this transcript decreased the transcription of emm and speBgenes and reduced the secretion of streptokinase. Enhanced Pel expression from a nisin-inducible plasmid resulted in increased message levels for emm in a wild-type organism. Characterization of the pel mutant provides evidence for the coordinated regulation of secreted and surface proteins and suggests the existence of a new global regulatory factor in S. pyogenes.

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supporting

confidence: 72%

Identification of pel , a Streptococcus pyogenes Locus That Affects both Surface and Secreted Proteins

Sledjeski

Kreikemeyer

et al. 1999

J Bacteriol

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“…Subsequent study established that proteolytic mechanism and specificity were conserved between Drosophila rhomboid and AarA64, and remarkably, interchanging their genes could rescue fly and bacterial signalling65. Moreover, although its identity remained unknown, the bacterial signal had biochemical properties consistent with being a small peptide66. Taken together, these observations dramatically suggested that activation of cell-to-cell signalling through rhomboid-mediated processing of precursor proteins might be the first signalling circuit known to be conserved between animals and bacteria65.…”

Section: Roles In Bacterial Pathogenesismentioning

confidence: 95%

Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms

Urban¹

2009

Nat Rev Microbiol

103

104

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PREFACEProteolysis in cellular membranes to liberate effector domains from their transmembrane anchors is a well-studied regulatory mechanism in animal biology and disease. By contrast, the function of intramembrane proteases in unicellular organisms has received little attention. Recent progress has now established that intramembrane proteases execute pivotal roles in a range of pathogens, from regulating Mycobacterium tuberculosis envelope composition, cholera toxin production, bacterial adherence and conjugation, to malaria parasite invasion, fungal virulence, immune evasion by parasitic amoebae and hepatitis C virus assembly. These advances raise the exciting possibility that intramembrane proteases may serve as targets for combating a wide range of infectious diseases. I focus on summarizing the advances, evaluating the limitations and highlighting the promise of this newly emerging field.Keywords cell signalling; regulated intramembrane proteolysis; rhomboid; site-2 protease; signal peptide peptidase; presenilin; invasion; malaria; hepatitis; cholera; tuberculosis INTRODUCTIONPathogens have evolved mechanisms to adapt quickly to the unreceptive environment of the host and establish a flourishing infection. Many of the events to which pathogens must respond occur at cellular membranes as sites of first contact. Work over the past decade has identified a novel class of membrane proteases that function to liberate effector domains from the membrane by cleaving transmembrane segments [1][2][3] . These intramembrane proteases are unusual polytopic enzymes; their active sites are assembled from residues on membranespanning segments, which embeds their water-dependent catalytic apparatus beneath the surface of the membrane.Intramembrane proteases are among the most conserved of all membrane proteins known, with members in all kingdoms of life [4][5][6] . Despite being widespread in unicellular organisms, without exception every intramembrane protease family was initially discovered through the study of metazoan biology or disease. Early examples of intramembrane proteolysis in unicellular organisms were relatively rare [7][8][9] , but this field has gained momentum, especially in the area of pathogens, and is coalescing into a new and distinct field. It is now established that intramembrane proteolysis is a fundamental biochemical mechanism used by a wide variety of pathogens to coordinate their infective cycles.Address for Correspondence: surban@jhmi.edu, Room 507 PCTB, 725 North Wolfe Street, Baltimore, Maryland, USA, 21205. NIH Public Access Author ManuscriptNat Rev Microbiol. Author manuscript; available in PMC 2010 June 1. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptIn this review, I will focus on the roles that intramembrane proteases have been discovered to play in pathogenic microorganisms, starting with bacterial pathogens, moving to pathogenic eukaryotes including protozoa and fungi, and closing with viruses. In comparing these examples, the challenge is to identify emergin...

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“…It is indeed likely that these enzymes have physiological functions in bacteria (acetylation, nucleotidylation, or phosphorylation of natural substrates) and that their activities against aminoglycosides in the wild-type strains are simply too weak to confer a phenotype of resistance. Yet, these proteins may be overexpressed under the pressure of aminoglycosides (84,112). In some cases, aminoglycosides may still remain poor substrates compared to the natural ones, but a moderate overexpression will nevertheless be enough to cause low-level resistance and further selection of the so-called intermediate susceptibility strains.…”

Section: Resistance Mechanismsmentioning

confidence: 99%

Aminoglycosides: Activity and Resistance

Mingeot‐Leclercq

Glupczynski

Tulkens

1999

Antimicrob Agents Chemother

806

498

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An extracellular factor regulating expression of the chromosomal aminoglycoside 2'-N-acetyltransferase of Providencia stuartii

Cited by 35 publications

References 45 publications

Identification of pel , a Streptococcus pyogenes Locus That Affects both Surface and Secreted Proteins

Identification of pel , a Streptococcus pyogenes Locus That Affects both Surface and Secreted Proteins

Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms

Aminoglycosides: Activity and Resistance

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