Identification of a Regulated Alkaline Phosphatase, a Cell Surface-Associated Lipoprotein, in Mycobacterium smegmatis
AUTOR(ES)
Kriakov, Jordan
FONTE
American Society for Microbiology
RESUMO
Although alkaline phosphatases are common in a wide variety of bacteria, there has been no prior evidence for alkaline phosphatases in Mycobacterium smegmatis. Here we report that transposon insertions in the pst operon, encoding homologues of an inorganic phosphate transporter, leads to constitutive expression of a protein with alkaline phosphatase activity. DNA sequence analysis revealed that M. smegmatis does indeed have a phoA gene that shows high homology to other phoA genes. The M. smegmatis phoA gene was shown to be induced by phosphate starvation and thus negatively regulated by the pst operon. Interestingly, the putative M. smegmatis PhoA has a hydrophobic N-terminal domain which resembles a lipoprotein signal sequence. The M. smegmatis PhoA was demonstrated to be an exported protein associated with the cell surface. Furthermore, immunoprecipitation of PhoA from [14C]acetate-labeled M. smegmatis cell lysates demonstrated that this phosphatase is a lipoprotein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=166462Documentos Relacionados
- Chloroplast Thylakoid Protein Phosphatase Is a Membrane Surface-Associated Activity 1
- Cell surface-associated structural proteins in connective tissue cells.
- Pattern formation by a cell surface-associated morphogen in Myxococcus xanthus
- Role of a cell surface-associated protein in adherence and dental caries.
- Identification and characterization of a surface-associated protein (Ssp) of Staphylococcus saprophyticus.