Heterogeneous Patterns of Acid Phosphatases Containing Low-Molecular-Mass Polypeptides in Members of the Family Enterobacteriaceae

Abstract

We investigated expression of acid phosphatases containing low-molecular-mass (25 to 27-ma) polypeptides (Lmmp-APs) similar to those described previously for Salmonella enterica serovar typhimurium and Morganella morganii in strains that were representatives of 43 different enterobacterial species by using a zymogram technique developed for detection of Lmmp-AP activities and for analysis of some of the properties of these enzymes. Under conditions that were suitable for detection of the previously described Lmmp-APs, production of similar enzymes appeared to be widespread but not universal among enteric bacteria, and heterogeneous patterns of expression were found among strains belonging to different genera and, in some cases, among strains belonging to different species of the same genus. We found that class A Lmmp-APs (i.e., Lmmp-Aps similar to the Morganella morganii PhoC and Salmonella enterica serovar typhimurium PhoN acid phosphatases) were also expressed in Cedecea spp., Enterobacter aerogenes, Hafiia alvei, Klebsiella spp., Providencia stuartii, Serratia plymuthica, and Yokenella regensburgei strains and that class B Lmmp-APs (i.e., Lmmp-APs similar to the Morganella morganii NapA and Salmonella enterica serovar typhimurium NapII acid phosphatases) were also expressed in strains of Citrobacter spp., Escherichia coli, Escherichia fergusonii, H a f i b alvei, Proteus mirabilis, Providenciu spp., Salmonella enterica serovar typhi, ShigeUa dysenteriae, and ShigeUa flexneri. No Lmmp-AP activity was detected in strains of Enterobacter spp. other than Enterobacter aerogenes, Escherichia hermanii, Kluyvera ascorbata, Leckrciu adecarboxyluta, Leminorella grimontii, MoellereUa wisconsensis, Proteus vulgaris, Proteus penneri, Serratia spp. other than Serratia plymuthica, and Yersinia spp. Because of the heterogeneous patterns of expression of Lmmp-APs, analysis of these enzymes could be useful for evolutionary studies of the enterobacterial genome and for precise phylogenetic positioning of enteric bacteria.Phosphatase activity occurs in all members of the family Enterobacteriaceae (18), but different patterns of phosphatase activity have been found in strains belonging to this family (2, 3, 10, 12, 13, 19). For instance, it is known that a phosphaterepressible alkaline phosphatase is widespread but not universally present in enterobacterial species (2, 13, 19). It is also known that the levels of cyclic phosphodiesterase activity and 5'-nucleotidase (UDP-sugar hydrolase) activity can be markedly different in different species (10) and that two different types of 5'-nucleotidases are produced by Escherichia coli and Salmonella spp. as a consequence of alternative silencing events in the genes that encode these enzymes (3). Moreover, only some species (Morganella morganii and Providencia stuartii) produce high levels of phosphate-irrepressible acid phosphatase activity (HPAP phenotype), while other species produce only intermediate or low levels of acid phosphatase activity when Pi is freely available in the cultu...

Agricultural uses of plant biostimulants

“…Acid phosphatases and phytases produced by rhizosphere microorganisms are involved in organic-P solubilization. Gram negative bacteria such as Pseudomonas, Burkholderia, Enterobacter, Citrobacter, and Serratia have been reported to produce acid phosphatases (Gügi et al 1991;Thaller et al 1995). Organic phosphate in soils is predominantly present as phytate, and production of the enzyme phytase by inoculants including Pseudomonas spp.…”

Genetics of phosphate solubilization and its potential applications for improving plant growth-promoting bacteria

“…Bacterial nonspecific acid phosphatases (phosphohydrolases) (NSAPs) are formed by three molecular families, which have been designated as molecular class A, B, and C (Thaller et al, 1995a). From their cellular location, these enzymes seem to function as organic phospho-ester scavengers, providing the cell with essential nutrients (releasing inorganic phosphates from nucleotides and sugar phosphates, for example, while the organic by-products are incorporated into the cell) (Beacham, 1980;Wanner, 1996).…”

The molecular class C acid phosphatase of Chryseobacterium meningosepticum (OlpA) is a broad-spectrum nucleotidase with preferential activity on 5′-nucleotides

“…Zymogram detection of the OlpA enzyme following SDS-PAGE and in-gel renaturation of proteins was performed using the phenolphthalein -methyl green detection system, as described previously [3,9]. Renaturation was carried out in 50 mM Tris -HCl (pH 7.0); equilibration and development for zymogram detection of the OlpA activity was carried out in 100 mM sodium acetate buffer (pH 6) containing 1 mM MgCl 2 .…”