Three Highly Homologous Membrane-bound Lipoproteins Participate in Oligopeptide Transport by the Ami System of the Gram-positive Streptococcus pneumoniae

Alloing, Geneviève; Philip, Pascale de; Claverys, Jean‐Pierre

doi:10.1006/jmbi.1994.1472

Cited by 129 publications

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“…The transport system from S. thermophilus consists of several different binding proteins, as in pathogenic streptococci (Alloing et al, 1994;Jenkinson et al, 1996), whereas that of L. lactis has only one binding protein. In each case, the presence of the binding protein is necessary for the transport function.…”

Section: Discussionmentioning

confidence: 99%

“…In S. gordonii, it has been proposed that peptide binding and subsequent uptake require the interaction between two binding proteins, HppA and HppP (Jenkinson et al, 1996). In contrast, interaction between binding proteins is not required for the peptidebinding function in S. pneumoniae: binding proteins are presumably acting independently (Alloing et al, 1994). This second model also applies to the Opt system of L. lactis, as the inactivation of optS does not impair the transport function of Opt (Lamarque et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…In S. thermophilus ST18, three highly homologous binding proteins (AmiA1, AmiA2 and AmiA3) are associated to a single translocon AmiCDEF. The presence of three distinct binding proteins has also been reported in other streptococci such as Streptococcus gordonii and Streptococcus pneumoniae (Alloing et al, 1994;Jenkinson et al, 1996). Nevertheless, these pathogenic streptococci are reported to transport peptides containing up to nine amino acid residues only.…”

Section: Introductionmentioning

confidence: 87%

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The specificity of oligopeptide transport by Streptococcus thermophilus resembles that of Lactococcus lactis and not that of pathogenic streptococci

2005

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Peptide transport is a crucial step in the growth of Streptococcus thermophilus in protein-or peptide-containing media. The objective of the present work was to determine the specificity of peptide utilization by this widely used lactic acid bacterium. To reach that goal, complementary approaches were employed. The capability of a proteinase-negative S. thermophilus strain to grow in a chemically defined medium containing a mixture of peptides isolated from milk as the source of amino acids was analysed. Peptides were separated into three size classes by ultrafiltration. The strain was able to use peptides up to 3?5 kDa during growth, as revealed by liquid chromatography and mass spectrometry analyses. The same strain was grown in chemically defined medium containing a tryptic digest of casein, and the respective time-course consumption of the peptides during growth was estimated. The ability to consume large peptides (up to 23 residues) was confirmed, as long as they are cationic and hydrophobic. These results were confirmed by peptide transport studies. Extension of the study to 11 other strains revealed that they all shared these preferences.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 87%

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The specificity of oligopeptide transport by Streptococcus thermophilus resembles that of Lactococcus lactis and not that of pathogenic streptococci

2005

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“…Thus, in addition to those described above, other solute-binding proteins from grampositive bacteria, i.e. for ribose (Woodson and Devine, 1994), maltose (Gilson et a]., 1988;Koivula et al, 1993), dipeptides (Mathiopoulos et al, 1991), oligopeptides (Alloing et al, 1994) and iron hydroxamate (Schneider and Hantke, 1993), are encoded by genes, the deduced products of which contain the consensus amino acid residues for the lipoprotein-cleavage site.…”

Section: Discussionmentioning

confidence: 99%

“…The latter are oriented towards the cytoplasm, and couple the hydrolysis of ATP to the transport process . In gram-negative bacteria, binding proteins are located in the periplasmic space, whereas in the few studied gram-positive bacteria, they were found linked to the surface of the cytoplasmic membrane by a lipid anchor (Alloing et al, 1994;Sutcliffe and Russell, 1995). The binding proteins are highly specific for interactions with various substrates, such as sugars, amino acids, oligopeptides and vitamins.…”

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A Lipid‐Anchored Binding Protein is a Component of an ATP‐Dependent Cellobiose/Cellotriose‐Transport System from the Cellulose Degrader Streptomyces reticuli

Schlösser

Schrempf

1996

European Journal of Biochemistry

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During cultivation in the presence of cellobiose or crystalline cellulose, Streptomyces reticuli expresses an inducible uptake system that transports cellobiose (K,,,, 4 pM), cellotriose and, to a lesser degree, cellotetraose and cellopentaose. Cellobiose uptake is dependent on ATP and inhibited by Nethylmaleimide. A binding protein was identified in its palmitylated form in the cytoplasmic membrane of mycelia. It could be extracted with the detergent Triton X-100 and purified by two subsequent anionexchange chromatographies. It showed highest affinity (&, 1 .5 pM) for cellobiose and cellotriose. The data suggest that cellobiose/cellotriose uptake is mediated by a membrane-anchored lipoprotein as a component of an ATP-binding-cassette-transporter system. Keywords : Streptomyces reticuli ; cellobiose/cellotriose transport ; vesicle ; lipoprotein ; uptake of glucose.Although Streptomycetes may utilize a number of sugars for growth, knowledge about the pathways of carbohydrate metabolism and their regulation is still limited (Romano, 1986). Transport studies indicated the presence of glucose-uptake systems in Streptomyces clavuligerus (Garcia-Dominguez et al., 1989), and an inducible cellobiose-transport system in Streptomyces grunaticolor (Jiresovg et al., 1987). The mechanisms for sugar uptake in Streptomycetes remain to be elucidated by means of biochemical and molecular-biological techniques. Recently a few Streptomyces sp. were shown to contain proteins that may belong to a fructose-specific phosphotransferase (PTS)system. However, a phosphoenolpyruvate-dependent transport of any sugar has not been demonstrated (Titgemeyer et al., 1995 ;Novotna and Hostalek, 1985). The cellobiose-uptake operons from Escherichiu coli (Kricker and Hall, 1987) and Bucillus stearothermophilus (Lai and Ingram, 1993) encode cellobiose-specific components of a PTS system.Within other bacteria, different types of sugar-transport systems have been identified. In addition to various PTS systems, binding-protein-dependent transport systems are encountered, which belong to the superfamily of ATP-binding-cassette transporters or traffic ATPases Higgins, 1992). These systems typically consist of five proteins (Ames, 1986): a soluble or membrane-associated binding protein ; two identical or similar integral membrane proteins; and two identical or similar ATP-binding proteins. The latter are oriented towards the cytoplasm, and couple the hydrolysis of ATP to the transport process . In gram-negative bacteria, binding proteins are located in the periplasmic space, whereas in the few studied gram-positive bacteria, they were found linked to the surface of the cytoplasmic membrane by a lipid anchor (Alloing et al., 1994;Sutcliffe and Russell, 1995 as sugars, amino acids, oligopeptides and vitamins. In addition to these binding-protein-dependent systems, bacteria contain secondary transport systems that couple the uptake of solutes to the proton-motive force (Krulwich, 1990).Previously, we identified a StreptomyceJ reticuli cellulace (Avicelase,...

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Encyclopedia of Molecular Biology

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Three Highly Homologous Membrane-bound Lipoproteins Participate in Oligopeptide Transport by the Ami System of the Gram-positive Streptococcus pneumoniae

Cited by 129 publications

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The specificity of oligopeptide transport by Streptococcus thermophilus resembles that of Lactococcus lactis and not that of pathogenic streptococci

The specificity of oligopeptide transport by Streptococcus thermophilus resembles that of Lactococcus lactis and not that of pathogenic streptococci

A Lipid‐Anchored Binding Protein is a Component of an ATP‐Dependent Cellobiose/Cellotriose‐Transport System from the Cellulose Degrader Streptomyces reticuli

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