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1.
Mol Microbiol ; 67(5): 947-57, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18194159

ABSTRACT

Quinones are essential components of the respiration chain that shuttle electrons between oxidoreductases. We characterized the quinones synthesized by Lactococcus lactis, a fermenting bacterium that activates aerobic respiration when a haem source is provided. Two distinct subgroups were characterized: Menaquinones (MK) MK-8 to MK-10, considered as hallmarks of L. lactis, are produced throughout growth. MK-3 and demethylMK-3 [(D)MK-3] are newly identified and are present only late in growth. Production of (D)MK-3 was conditional on the carbon sugar and on the presence of carbon catabolite regulator gene ccpA. Electron flux driven by both (D)MK fractions was shared between the quinol oxidase and extracellular acceptors O(2), iron and, with remarkable efficiency, copper. Purified (D)MK-3, but not MK-8-10, complemented a menB defect in L. lactis. We previously showed that a respiratory metabolism is activated in Group B Streptococcus (GBS) by exogenous haem and MK, and that this activity is implicated in virulence. Here we show that growing lactococci donate (D)MK to GBS to activate respiration and stimulate growth of this opportunist pathogen. We propose that conditions favouring (D)MK production in dense microbial ecosystems, as present in the intestinal tract, could favour implantation of (D)MK-scavengers like GBS within the complex.


Subject(s)
Lactococcus lactis/metabolism , Quinones/analysis , Quinones/metabolism , Bacterial Proteins/metabolism , Chromatography, High Pressure Liquid , Copper/metabolism , DNA-Binding Proteins/metabolism , Electron Transport , Glycoside Hydrolases/metabolism , Iron/metabolism , Lactococcus lactis/growth & development , Mutation , Oxidative Stress , Oxygen/metabolism , Repressor Proteins/metabolism , Streptococcus agalactiae/growth & development , Vitamin K 2/analysis , Vitamin K 2/metabolism
2.
Nat Genet ; 34(2): 154-6, 2003 Jun.
Article in English | MEDLINE | ID: mdl-12730697

ABSTRACT

Autosomal dominant hypercholesterolemia (ADH; OMIM144400), a risk factor for coronary heart disease, is characterized by an increase in low-density lipoprotein cholesterol levels that is associated with mutations in the genes LDLR (encoding low-density lipoprotein receptor) or APOB (encoding apolipoprotein B). We mapped a third locus associated with ADH, HCHOLA3 at 1p32, and now report two mutations in the gene PCSK9 (encoding proprotein convertase subtilisin/kexin type 9) that cause ADH. PCSK9 encodes NARC-1 (neural apoptosis regulated convertase), a newly identified human subtilase that is highly expressed in the liver and contributes to cholesterol homeostasis.


Subject(s)
Hyperlipoproteinemia Type II/genetics , Mutation , Serine Endopeptidases/genetics , Amino Acid Substitution , Chromosomes, Human, Pair 1/genetics , Female , Genes, Dominant , Genetic Linkage , Humans , Hyperlipoproteinemia Type II/enzymology , Liver/enzymology , Male , Pedigree , Proprotein Convertase 9 , Proprotein Convertases
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