Diversity and Evolution of Protein Translocation

Pohlschröder, Mechthild; Hartmann, Enno; Hand, Nicholas J.; Dilks, Kieran; Haddad, Alex

doi:10.1146/annurev.micro.59.030804.121353

Cited by 109 publications

(76 citation statements)

References 126 publications

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“…However, this pathway is unlikely to be present in GAS due to the absence of homologues of conserved components of this pathway (Dilks et al, 2003). A possible alternative to the GAS SRP pathway may involve the YidC/Oxa1/Alb3 family of proteins (Pohlschroder et al, 2005). Members of the YidC/Oxa1/Alb3 family of proteins are involved in the insertion of proteins into the membranes of bacteria, mitochondria and chloroplasts, respectively.…”

Section: Discussionmentioning

confidence: 99%

The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence

2010

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The signal recognition particle (SRP) is a ribonucleoprotein complex that targets proteins for secretion in a co-translational manner. While originally thought to be essential in all bacteria, recent data show that the SRP is dispensable in at least some streptococcal species. The SRP from the human pathogen group A Streptococcus (GAS, Streptococcus pyogenes) is predicted to be composed of protein Ffh and 4.5S RNA. Deletion of ffh alters the secretion of several GAS proteins, and leads to a severe reduction in virulence. Here, we report that mutation of the gene encoding 4.5S RNA results in phenotypes both similar to and distinct from that observed following ffh mutation. Similarities include a reduction in secretion of the haemolysin streptolysin O, and attenuation of virulence as assessed by a murine soft tissue infection model. Differences include a reduction in transcript levels for the genes encoding streptolysin O and NADglycohydrolase, and the reduced secretion of the SpeB protease. Several differences in transcript abundance between the parental and mutant strain were shown to be dependent on the sensorkinase-encoding gene covS. Using growth in human saliva as an ex vivo model of upper respiratory tract infection we identified that 4.5S RNA mutation leads to a 10-fold reduction in colony-forming units over time, consistent with the 4.5S RNA contributing to GAS growth and persistence during upper respiratory tract infections. Finally, we determined that the 4.5S RNA was essential for GAS to cause lethal infections in a murine bacteraemia model of infection. The data presented extend our knowledge of the contribution of the SRP to the virulence of an important Gram-positive pathogen.

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Section: Discussionmentioning

confidence: 99%

The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence

2010

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“…32,33 Ribosomeassociated SRP recognizes and binds signal peptides of nascent secretory or membrane proteins (in eukaryotes) or integral plasma membrane proteins (in prokaryotes; Figure 1). The ribosome-nascent chain complex is then targeted by SRP to the SRP receptor, which is anchored to the membrane.…”

Section: The Srp-dependent Targeting Cycle In Eukaryotes and Prokaryotesmentioning

confidence: 99%

Use of synthetic signal sequences to explore the protein export machinery

Clérico¹,

Maki²,

Gierasch³

2008

Biopolymers

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The information for correct localization of newly synthesized proteins in both prokaryotes and eukaryotes resides in self‐contained, often transportable targeting sequences. Of these, signal sequences specify that a protein should be secreted from a cell or incorporated into the cytoplasmic membrane. A central puzzle is presented by the lack of primary structural homology among signal sequences, although they share common features in their sequences. Synthetic signal peptides have enabled a wide range of studies of how these “zipcodes” for protein secretion are decoded and used to target proteins to the protein machinery that facilitates their translocation across and integration into membranes. We review research on how the information in signal sequences enables their passenger proteins to be correctly and efficiently localized. Synthetic signal peptides have made possible binding and crosslinking studies to explore how selectivity is achieved in recognition by the signal sequence‐binding receptors, signal recognition particle, or SRP, which functions in all organisms, and SecA, which functions in prokaryotes and some organelles of prokaryotic origins. While progress has been made, the absence of atomic resolution structures for complexes of signal peptides and their receptors has definitely left many questions to be answered in the future. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 307–319, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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“…Attempts to elucidate the insertion requirements for this mutant in vitro were unsuccessful because of the proteinase K-resistant nature of the protein. 3 Substitution of a glycine for aspartate in TM1 of F o c results in a mutant form of the protein that is still dependent of YidC for insertion but that does not form an oligomeric ring structure as the wild type protein does (32,48). Thus the introduction of a negative charge into a TMS is tolerated by the YidC-only mode of insertion.…”

Section: Discussionmentioning

confidence: 99%

“…YidC belongs to the evolutionarily conserved Oxa1/Alb3/YidC family. Oxa-related proteins have been identified in all genomes sequenced to date and are postulated to have evolved before the divergence of the three major domains of life (3)(4)(5). Oxa1 (oxidase assembly) from yeast was the first member of this family to be described (6,7).…”

mentioning

confidence: 99%

Conserved Negative Charges in the Transmembrane Segments of Subunit K of the NADH:Ubiquinone Oxidoreductase Determine Its Dependence on YidC for Membrane Insertion

Driessen

2010

Journal of Biological Chemistry

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All members of the Oxa1/Alb3/YidC family have been implicated in the biogenesis of respiratory and energy transducing proteins. In Escherichia coli, YidC functions together with and independently of the Sec system. Although the range of proteins shown to be dependent on YidC continues to increase, the exact role of YidC in insertion remains enigmatic. Here we show that YidC is essential for the insertion of subunit K of the NADH: ubiquinone oxidoreductase and that the dependence is due to the presence of two conserved glutamate residues in the transmembrane segments of subunit K. The results suggest a model in which YidC serves as a membrane chaperone for the insertion of the less hydrophobic, negatively charged transmembrane segments of NuoK.

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Diversity and Evolution of Protein Translocation

Cited by 109 publications

References 126 publications

The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence

The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence

Use of synthetic signal sequences to explore the protein export machinery

Conserved Negative Charges in the Transmembrane Segments of Subunit K of the NADH:Ubiquinone Oxidoreductase Determine Its Dependence on YidC for Membrane Insertion

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