Reconstitution of maltose chemotaxis in Escherichia coli by addition of maltose-binding protein to calcium-treated cells of maltose regulon mutants

Brass, J M; Manson, Michael D.

doi:10.1128/jb.157.3.881-890.1984

Cited by 47 publications

(11 citation statements)

References 50 publications

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“…5). To normalize the results of capillary tests for possible differences in the motility or chemotactic ability of cells following reconstitution, we expressed the accumulations in maltose-containing capillaries as a percentage of the accumulations in aspartatecontaining capillaries (7). The rationale for this normalization procedure is that both the aspartate and maltose responses in E. coli are mediated by the Tar signal transducer.…”

Section: Methodsmentioning

confidence: 99%

Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria

Dahl¹,

Manson²

1985

J Bacteriol

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In Escherichia coli, the periplasmic maltose-binding protein (MBP), the product of the malE gene, is the primary recognition component of the transport system for maltose and maltodextrins. It is also the maltose chemoreceptor, in which capacity it interacts with the signal transducer Tar (taxis to aspartate and some repellents). In studies of the maltose system in other members of the family Enterobacteriaceae, we found that MBP is produced by Salmonella typhimurium, Klebsiella pneumoniae, Enterobacter aerogenes, and Serratia marcescens. MBP from all of these species cross-reacted with antibody against the E. coli protein and had a similar molecular weight (about 40,000). The Shigella flexneri and Proteus mirabilis strains we examined did not synthesize MBP. The isoelectric points of MBP from different species varied from the acid extreme of E. coli (4.8) to the basic extreme of E. aerogenes (8.9). All species with MBP transported maltose with high affinity, although the Vmax for K. pneumoniae was severalfold lower than that for the other species. Maltose chemotaxis was observed only in E. coli and E. aerogenes. In S. typhimurium LT2, Tar was completely inactive in maltose taxis, although it signaled normally in response to aspartate. MBP isolated from all five species could be used to reconstitute maltose transport and taxis in a delta malE strain of E. coli after permeabilization of the outer membrane with calcium.

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Section: Methodsmentioning

confidence: 99%

Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria

Dahl¹,

Manson²

1985

J Bacteriol

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“…MBP and GBP were purified from the overproducing E. coli strains MM129 (Brass and Manson, 1984) and U\5709 (provided by W. Boos) carrying piasmids pMK3 [maiE') (provided by M. Manson) and pBDIO [mgIB') (provided by D. Benner), respectively, GBP vi/as purified according to Anraku (1968). MBP vt/as purified by affinity chromatography on amylose (Ferenci and Klotz, 1978).…”

Section: Labelling Of Proteinsmentioning

confidence: 99%

“…In order to determine whether the morphological subcompartments formed by the periseptal annuli act as barriers to the free movement of periplasmic proteins, we have adapted the technique of fluorescence recovery after photobleaching (FRAP). The approach is based on our previous demonstration that proteins labelled with fluorescent probes can be introduced into the periplasmic space of living bacteria without any apparent disruption of cellular function (Brass ef al., 1983;Brass and Manson, 1984;Brass, 1986a). By irreversibly bleaching a local area of the periplasm using a laser, and following the recovery of fluorescence (i.e.…”

Section: Introductionmentioning

confidence: 99%

Compartmentalization of the periplasm at cell division sites in Escherichia coli as shown by fluorescence photobleaching experiments

Foley

Brass

Birmingham

et al. 1989

Molecular Microbiology

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Morphological evidence has previously indicated that the periplasmic space of Escherichia coli is compartmentalized at sites corresponding to future sites of cell division. The borders of these morphological compartments are formed by localized zones of adhesion (periseptal annuli). In the present study, the technique of fluorescence recovery after photobleaching was used to determine whether these structures act as barriers to the free movement of proteins within the periplasm. The recovery of fluorescence in the ftsA filaments was found to be uniformly low over at potential sites of cell division and at the cell poles, indicating that these regions are biochemically sequestered from the remainder of the periplasmic space. Our results provide direct evidence for local compartments within the periplasm, primarily located at the sites of past or future cell divisions. The implications of this finding for cell division and other periplasmic processes are discussed.

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“…Tar and Tsr bind aspartate and serine, respectively (Mesibov and Adler, 1972;. Other attractants, such as sugars and dipeptides, are recognized by periplasmic binding proteins that interact with particular transducers: maltose-binding protein (MBP) with Tar (Hazelbauer, 1975;Brass and Manson, 1984), dipeptide-binding protein (DBP) with Tap (Manson etal., 1986;Abouhamad eta/., 1991) and galactose/glucose-binding protein (GBP) and ribose-binding protein (RBP) with Trg (Hazelbauer and Adler, 1971;Aksamit and Koshland, 1974).…”

Section: Introductionmentioning

confidence: 99%

Maltose‐binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor

Gardina

Bormans

Hawkins

et al. 1997

Molecular Microbiology

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SummaryThe Tar chemotactic signal transducer of Escherichia coli mediates attractant responses to L-aspartate and to maltose. Aspartate binds across the subunit interface of the periplasmic receptor domain of a Tar homodimer. Maltose, in contrast, first binds to the periplasmic maltose-binding protein (MBP), which in its ligand-stabilized closed form then interacts with Tar. lntragenic complementation was used to determine the MBP-binding site on the Tar dimer. Mutations causing certain substitutions at residues Tyr-143, Asn-145, Gly-147, Tyr-149, and Phe-150 of Tar lead to severe defects in maltose chemotaxis, as do certain mutations affecting residues Arg-73, Met-76, Asp-77, and Ser-83. These two sets of mutations defined two complementation groups when the defective proteins were co-expressed at equal levels from compatible plasmids. We conclude that MBP contacts both subunits of the Tar dimer simultaneously and asymmetrically. Mutations affecting Met-75 could not be complemented, suggesting that this residue is important for association of MBP with each subunit of the Tar dimer. When the residues involved in interaction with MBP were mapped onto the crystal structure of the Tar periplasmic domain, they localized to a groove at the membrane-distal apex of the domain and also extended onto one shoulder of the apical region.

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Reconstitution of maltose chemotaxis in Escherichia coli by addition of maltose-binding protein to calcium-treated cells of maltose regulon mutants

Cited by 47 publications

References 50 publications

Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria

Interspecific reconstitution of maltose transport and chemotaxis in Escherichia coli with maltose-binding protein from various enteric bacteria

Compartmentalization of the periplasm at cell division sites in Escherichia coli as shown by fluorescence photobleaching experiments

Maltose‐binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor

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