Phosphoproteins and the phosphoenolpyruvate: sugar phosphotransferase system of <i>Streptococcus salivarius</i>. Detection of two different ATP-dependent phosphorylations of the phosphocarrier protein HPr

Eb, Waygood; Rl, Mattoo; E, Erickson; Vadeboncoeur, Christian

doi:10.1139/m86-062

Cited by 31 publications

(16 citation statements)

References 33 publications

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“…Phosphorylation of HPr on Ser-46 has been reported in the oral streptococci, Streptococcus mutans and Streptococcus salivarius (Waygood et al, 1986;Mimura et al, 1987;Vadeboncoeur et al, 1991). Results so far obtained in oral streptococci with respect to this phosphorylation reaction have revealed some peculiarities.…”

Section: Introductionmentioning

confidence: 94%

Replacement of isoleucine‐47 by threonine in the HPr protein of Streptococcus salivarius abrogates the preferential metabolism of glucose and fructose over lactose and melibiose but does not prevent the phosphorylation of HPr on serine‐46

Gauthier

Brochu

Eltis

et al. 1997

Molecular Microbiology

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Section: Introductionmentioning

confidence: 94%

Replacement of isoleucine‐47 by threonine in the HPr protein of Streptococcus salivarius abrogates the preferential metabolism of glucose and fructose over lactose and melibiose but does not prevent the phosphorylation of HPr on serine‐46

Gauthier

Brochu

Eltis

et al. 1997

Molecular Microbiology

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“…Phosphorylation by purified (Ser)HPr kinases from S. pyogenes, Enterococcus faecalis, B. subtilis, and L. brevis (23,26) is stimulated by fructose-1,6-bisphosphate (FBP) and inhibited by P i . (Ser)HPr kinase activity has been observed in the oral species, Streptococcus salivarius (34,37) and Streptococcus mu-tans (21,34), and activity of the enzyme in the latter organism has also been shown to be activated by FBP and inhibited by P i and some glycolytic intermediates (21).…”

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confidence: 99%

Regulation of ATP-dependent P-(Ser)-HPr formation in Streptococcus mutans and Streptococcus salivarius

et al. 1995

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Sugar transport via the phosphoenolpyruvate (PEP) phosphotransferase system involves PEP-dependent phosphorylation of the general phosphotransferase system protein, HPr, at histidine 15. However, grampositive bacteria can also carry out ATP-dependent phosphorylation of HPr at serine 46 by means of (Ser)HPr kinase. In this study, we demonstrate that (Ser)HPr kinase in crude preparations of Streptococcus mutans Ingbritt and Streptococcus salivarius ATCC 25975 is membrane associated, with pH optima of 7.0 and 7.5, respectively. The latter organism possessed 7-to 27-fold-higher activity than S. mutans NCTC 10449, GS-5, and Ingbritt strains. The enzyme in S. salivarius was activated by fructose-1,6-bisphosphate (FBP) twofold with 0.05 mM ATP, but this intermediate was slightly inhibitory with 1.0 mM ATP at FBP concentrations up to 10 mM. Similar inhibition was observed with the enzyme from S. mutans Ingbritt. A variety of other glycolytic intermediates had no effect on kinase activity under these conditions. The activity and regulation of (Ser)HPr kinase were assessed in vivo by monitoring P- ( The principal sugar transport system in oral streptococci is the phosphoenolpyruvate (PEP):sugar phosphotransferase transport system (PTS) (33). The PTS is a group translocation process which utilizes PEP for the phosphorylation of incoming sugars via a phosphoryl transfer process involving the general, non-sugar-specific proteins enzyme I (EI) and HPr and subsequently a sugar-specific, membrane-bound enzyme II (EII) complex, which catalyzes the transport and phosphorylation of the specific carbohydrate (22). During this process, HPr is transiently phosphorylated by P-EI on histidyl residue 15 (His-15) and the phosphate group from phospho-HPr [Pϳ(His)-HPr] is then transferred to the membrane-bound EII complex. The EII complex consists of three functional domains: (i) the IIA domain (also referred to as enzyme III) possessing the first phosphorylation site, (ii) the IIB domain bearing the second phosphorylation site, and (iii) the IIC domain that forms the transmembrane channel and provides the sugar-binding site (30).In 1983, Deutscher and Saier (5) showed that the HPr of Streptococcus pyogenes could also be phosphorylated on a serine residue at the expense of ATP by a specific HPr kinase. This phosphorylation reaction was subsequently found to be widespread among gram-positive but not gram-negative bacteria (22,27) and has even been shown to occur in some species lacking a functional PTS (27). Whereas several observations over the past 10 years have suggested that P-(Ser)-HPr possesses regulatory roles, only recently have some of the physiological functions of this phosphoprotein been determined. These functions include the regulation of glucose and lactose permease activity in Lactobacillus brevis (38, 39), regulation of inducer expulsion in Lactococcus lactis (40), and involvement in catabolite repression in Bacillus subtilis (4). In vitro studies have suggested that the intracellular concentration of P-(Ser)-HPr is contro...

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“…At least two kinase-phosphorylated proteins have been identified as to function in Escherichia coli, isocitrate dehydrogenase [5,6] and RNA polymerase [7], and one such protein has been identified in several gram-positive species as a heat-stable phosphocarrier protein, HPr, of the bacterial sugar phosphotransferase system [4,8,9]. Protein kinases have been purified from E coli [7,10], from Streptococcus fuecalis [ll] and have been partially purified from Streptococcus pyogenes [8].…”

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ATP‐dependent protein kinase activities in the oral pathogen Streptococcus mutans

Mimura

Poy

Jacobson

1987

J of Cellular Biochemistry

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ATP-dependent protein kinase activities were detected in both membrane and cytoplasmic fractions from the oral pathogen Streptococcus mutans. Different polypeptides were phosphorylated by endogenous kinase(s) in the two fractions. In membranes, five phosphoproteins were detected with apparent masses of 82, 37, 22, 12, and 10 kilodaltons (KD). In cytoplasm, two major acid-stable phosphoproteins were found. One was identified as HPr of the phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS), while the other had an apparent mass of 61 KD. Both of these proteins were phosphorylated on a seryl residue. Fructose 1,6-bisphosphate stimulated phosphorylation of HPr by the kinase and inhibited phosphorylation of the 61-KD protein. In contrast, fructose 1-phosphate, 2-phosphoglycerate, 3-phosphoglycerate, and dihydroxyacetone phosphate inhibited phosphorylation of HPr and stimulated phosphorylation of the 61-KD protein. Several other glycolytic intermediates as well as inorganic phosphate inhibited phosphorylation of either or both proteins. Preincubation of cytoplasm with PEP prior to incubation with ATP reduced the amount of phospho-(seryl)-HPr formed, but not that of the 61-KD phosphoprotein. The latter protein has not yet been identified but has properties that suggest that it may be the protein kinase itself. These results provide evidence for one or more soluble ATP-dependent protein kinases in S mutans that are regulated by glycolytic intermediates and that may play a role in the modulation of carbohydrate uptake and metabolism in this organism. A model for feedback regulation of sugar transport in S mutans, mediated by an allosterically regulated kinase, is presented.

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Phosphoproteins and the phosphoenolpyruvate: sugar phosphotransferase system of Streptococcus salivarius. Detection of two different ATP-dependent phosphorylations of the phosphocarrier protein HPr

Cited by 31 publications

References 33 publications

Replacement of isoleucine‐47 by threonine in the HPr protein of Streptococcus salivarius abrogates the preferential metabolism of glucose and fructose over lactose and melibiose but does not prevent the phosphorylation of HPr on serine‐46

Replacement of isoleucine‐47 by threonine in the HPr protein of Streptococcus salivarius abrogates the preferential metabolism of glucose and fructose over lactose and melibiose but does not prevent the phosphorylation of HPr on serine‐46

Regulation of ATP-dependent P-(Ser)-HPr formation in Streptococcus mutans and Streptococcus salivarius

ATP‐dependent protein kinase activities in the oral pathogen Streptococcus mutans

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