Enzymes II of the phospho enol pyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transport

Lengeler, Joseph W.; Jahreis, Knut; Wehmeier, Udo F.

doi:10.1016/0005-2728(94)90017-5

Cited by 129 publications

(142 citation statements)

References 172 publications

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“…All the residues mentioned above that are conserved in all so far known transporters of the Glc-Nag subfamily (G149, R203, H 211, G295, TE 297/298, D343) or at least in the glucose transporters (M17, H212, I296) are shaded. Sequence analysis of the two EIICBA Glc from S. carnosus suggests a complete agreement with the proposed two-dimensional structure of IIC from E. coli, according to the model from Lengeler et al (1994).…”

Section: Figsupporting

confidence: 73%

“…This system has also been implicated in chemotaxis and in regulation of numerous catabolic pathways (Erni, 1992 ;Hengstenberg et al, 1993 ;Postma et al, 1993 ;Lengeler et al, 1994). Enzyme I (EI) and the histidine-containing phosphocarrier protein (HPr) are soluble cytoplasmic proteins that are involved in the transport of all PTS sugars and are thus designated as general proteins of the PTS.…”

Section: Introductionmentioning

confidence: 99%

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Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system – two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?

Christiansen

Hengstenberg

1999

Microbiology

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Previous sequence analysis of the glucose-specific PTS gene locus from Staphylococcus carnosus revealed the unexpected finding of two adjacent, highly similar ORFs, glcA and glcB, each encoding a glucose-specific membrane permease EIICBA Glc . glcA and glcB show 73 % identity at the nucleotide level and glcB is located 131 bp downstream from glcA. Each of the genes is flanked by putative regulatory elements such as a termination stem-loop, promoter and ribosome-binding site, suggesting independent regulation. The finding of putative cis-active operator sequences, CRE (catabolite-responsive elements) suggests additional regulation by carbon catabolite repression. As described previously by the authors, both genes can be expressed in Escherichia coli under control of their own promoters. Two putative promoters are located upstream of glcA, and both were found to initiate transcription in E. coli.

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Section: Figsupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system – two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?

Christiansen

Hengstenberg

1999

Microbiology

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“…glycosid.txt and http :\\afmb.cnrs-mrs.fr\"cazy\ CAZY\index.html). By their composition and modular structure, proteins MalB, GlvA and AglA, can be assigned to the EII Glc/Scr family of PTS transporters (Lengeler et al, 1994 ;Lanz & Erni, 1998 (Robrish et al, 1991 ;Thompson et al, 1992). Because sucrose and its isomers comprise the same hexose moieties, it was of interest to determine whether sucrose-grown cells of F. mortiferum would also metabolize the isomeric compounds.…”

Section: Sequence Alignment Of Phospho-α-glucosidase and Eii(cb) Protmentioning

confidence: 99%

Metabolism of sucrose and its five isomers by Fusobacterium mortiferum

et al. 2002

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Fusobacterium mortiferum utilizes sucrose [glucose-fructose in α(1 2) linkage] and its five isomeric α-D-glucosyl-D-fructoses as energy sources for growth.Sucrose-grown cells are induced for both sucrose-6-phosphate hydrolase (S6PH) and fructokinase (FK), but the two enzymes are not expressed above constitutive levels during growth on the isomeric compounds. Extracts of cells grown previously on the sucrose isomers trehalulose α(1 1), turanose α(1 3), maltulose α(1 4), leucrose α(1 5) and palatinose α(1 6) contained high levels of an NAD M plus metal-dependent phospho-α-glucosidase (MalH). The latter enzyme was not induced during growth on sucrose. MalH catalysed the hydrolysis of the 6'-phosphorylated derivatives of the five isomers to yield glucose 6-phosphate and fructose, but sucrose 6-phosphate itself was not a substrate. Unexpectedly, MalH hydrolysed both α-and β-linked stereomers of the chromogenic analogue p-nitrophenyl glucoside 6-phosphate. The gene malH is adjacent to malB and malR, which encode an EII(CB) component of the phosphoenolpyruvate-dependent sugar :phosphotransferase system and a putative regulatory protein, respectively. The authors suggest that for F. mortiferum, the products of malB and malH catalyse the phosphorylative translocation and intracellular hydrolysis of the five isomers of sucrose and of related α-linked glucosides. Genes homologous to malB and malH are present in both Klebsiella pneumoniae and the enterohaemorrhagic strain Escherichia coli O157 :H7. Both these organisms grew well on sucrose, but only K. pneumoniae exhibited growth on the isomeric compounds.

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“…involved in phosphoryl group transfer (Lengeler et al, 1994). The permeases are in most cases co-transcribed with the downstream phospho-β-glucosidase and the expression is regulated by catabolite repression mediated by the general PTS proteins, and specific induction by the β-glucoside substrates which prevents negative regulation by IIAB (Rutberg, 1997 ;Stu$ lke et al, 1998).…”

Section: Amino Acid Homology Of the Overexpressed Fragmentsmentioning

confidence: 99%

Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative β-glucoside-specific PTS system The EMBL accession numbers for the sequences reported in this paper are AJ251202, AJ251203 and AJ251204.

Gravesen¹,

Warthoe²,

Knøchel³

et al. 2000

Microbiology

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Pediocin PA-1, which is a bacteriocin produced by lactic acid bacteria, has potential as a biopreservative of food. However, such use may lead to the development of resistance in the target organism. Gene expression in two independent pediocin-resistant mutants of Listeria monocytogenes 412 was compared to the original isolate by restriction fragment differential display PCR (RFDD-PCR). This method amplifies cDNA restriction fragments under stringent PCR conditions, enabled by the use of specific primers complementary to ligated adaptor sequences. RFDD-PCR was very well suited for analysis of listerial gene expression, giving reproducible PCR product profiles. Three gene fragments having increased expression in both resistant mutants were identified. All three had homology to components of β-glucoside-specific phosphoenolpyruvate-dependent phosphotransferase systems (PTS), one fragment having homology to enzyme II permeases, and the two others to phospho-β-glucosidases. Overexpression of the putative PTS system was consistently observed in 10 additional pediocin-resistant mutants, isolated at different pH, salt content and temperature. The results suggest that RFDD-PCR is a strong approach for the analysis of prokaryotic gene expression and that the putative β-glucoside-specific PTS system is involved in mediating pediocin resistance.

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Enzymes II of the phospho enol pyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transport

Cited by 129 publications

References 172 publications

Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system – two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?

Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system – two highly similar glucose permeases in Staphylococcus carnosus with different glucoside specificity: protein engineering in vivo?

Metabolism of sucrose and its five isomers by Fusobacterium mortiferum

Restriction fragment differential display of pediocin-resistant Listeria monocytogenes 412 mutants shows consistent overexpression of a putative β-glucoside-specific PTS system The EMBL accession numbers for the sequences reported in this paper are AJ251202, AJ251203 and AJ251204.

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