First evidences for a third sulfatase maturation system in prokaryotes from E. coli aslB and ydeM deletion mutants.
To be active all known arylsulfatases undergo a unique post-translational modification leading to the conversion of an active site residue (serine or cysteine) into a C(alpha)-formylglycine. Although deprived of sulfatase activity, Escherichia coli K12 can efficiently mature heterologous Cys-type sulfatases. Three potential enzymes (AslB, YdeM and YidF) belonging to the anaerobic sulfatase maturating enzyme family (an SME) are present in its genome. Here we show that E. coli could mature Cys-type sulfatases only in aerobic conditions and that knocking-out of aslB, ydeM and yidF does not impair Cys-type sulfatase maturation. These findings demonstrate that these putative anSME are not involved in Cys-type sulfatase maturation and strongly support the existence of a second, oxygen-dependent and Cys-type specific sulfatase maturation system among prokaryotes.
Benjdia
Alhosna
A
INRA, Unité d'Ecologie et Physiologie du Système Digestif, 78352 Jouy-en-Josas, France.
Dehò
Gianni
G
Rabot
Sylvie
S
Berteau
Olivier
O
D000595:Amino Acid Sequence; D001192:Arylsulfatases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D020134:Catalytic Domain / Q000235:genetics; D003545:Cysteine / Q000737:chemistry; D048168:Escherichia coli K12 / Q000201:enzymology* / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017353:Gene Deletion; D005798:Genes, Bacterial; D008954:Models, Biological; D008969:Molecular Sequence Data; D009876:Operon; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000737:chemistry
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D012694:Serine; D001192:Arylsulfatases; D003545:Cysteine