title: Streptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2.
abstract: The signal recognition particle (SRP)-translocation pathway is conserved in all three domains of life and delivers membrane and secretory proteins to the cytoplasmic membrane or endoplasmic reticulum. We determined the requirement in the cariogenic oral pathogen Streptocococcus mutans of the three universally conserved elements of the SRP pathway: Ffh/SRP54, scRNA, and FtsY/SRalpha. Previously, we reported that insertional interruption of S. mutans ffh was not lethal, but resulted in acid sensitivity. To test whether S. mutans could survive extensive disruption of the SRP pathway, single and double deletions of genes encoding Ffh, scRNA, and FtsY were generated. Without environmental stressors, all mutant strains were viable, but unlike the wild-type, none could initiate growth at pH 5.0 or in 3.5% NaCl. Survival of challenge with 0.3 mM H(2)O(2) was also diminished without ffh. Members of the YidC/Oxa1/Alb3 family are also ubiquitous, involved in the translocation and assembly of membrane proteins, and have been identified in prokaryotes/mitochondria/chloroplasts. Two genes encoding YidC homologs, YidC1 and YidC2, are present in streptococcal genomes with both expressed in S. mutans. Deletion of YidC1 demonstrated no obvious phenotype. Elimination of YidC2 resulted in a stress-sensitive phenotype similar to SRP pathway mutants. Mutants lacking both YidC2 and SRP components were severely impaired and barely able to grow, even in the absence of environmental stress. Here, we report the dispensability of the cotranslational SRP protein translocation system in a bacterium. In S. mutans, this pathway contributes to protection against rapid environmental challenge and may overlap functionally with YidC2.
authors.affiliation: Department of Oral Biology, University of Florida, Gainesville, FL 32610, USA.
authors.forename: Adnan
authors.initials: A
authors.lastname: Hasona
authors.forename: Paula J
authors.initials: PJ
authors.lastname: Crowley
authors.forename: Celine M
authors.initials: CM
authors.lastname: Levesque
authors.forename: Richard W
authors.initials: RW
authors.lastname: Mair
authors.forename: Dennis G
authors.initials: DG
authors.lastname: Cvitkovitch
authors.forename: Arnold S
authors.initials: AS
authors.lastname: Bleiweis
authors.forename: L Jeannine
authors.initials: LJ
authors.lastname: Brady
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics; D002470:Cell Survival / Q000187:drug effects / Q000235:genetics; D003001:Cloning, Molecular; D005816:Genetic Complementation Test; D006861:Hydrogen Peroxide / Q000633:toxicity; D006863:Hydrogen-Ion Concentration; D026901:Membrane Transport Proteins / Q000235:genetics*; D016296:Mutagenesis; D018384:Oxidative Stress / Q000235:genetics; D006180:Proton-Translocating ATPases / Q000378:metabolism; D020733:RNA, Small Cytoplasmic / Q000235:genetics; D018160:Receptors, Cytoplasmic and Nuclear / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D018271:Signal Recognition Particle / Q000235:genetics* / Q000502:physiology*; D015398:Signal Transduction / Q000235:genetics*; D013295:Streptococcus mutans / Q000187:drug effects / Q000235:genetics* / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; C087406:FtsY protein, Bacteria; D026901:Membrane Transport Proteins; D020733:RNA, Small Cytoplasmic; D018160:Receptors, Cytoplasmic and Nuclear; D018271:Signal Recognition Particle; D006861:Hydrogen Peroxide; D006180:Proton-Translocating ATPases