A transmembrane signalling complex controls transcription of the Uhp sugar phosphate transport system

Kadner, Robert J.; Island, Michael D.; Dahl, John L.; Webber, Carol A.

doi:10.1016/0923-2508(94)90085-x

Cited by 24 publications

(23 citation statements)

References 20 publications

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“…UhpC has already been identified as a protein with substantial structural similarities to the E. coli Glc6P transporter UhpT (15). Interestingly, the chlamydial HPTcp protein exhibits 45% identity to the Glc6P sensor protein UhpC, which is significantly higher than that to the Glc6P transporter UhpT (see above).…”

Section: Structural Characteristics Of Uhpc and Hptcpmentioning

confidence: 94%

“…UhpT is a typical member of the major facilitator superfamily (MFS) that is predicted to have 12 ␣-helical transmembrane domains (17). The amino acid sequence of the E. coli UhpC protein exhibits 32% identity to the transport protein UhpT and both proteins share the same predicted transmembrane topology (15). It is proposed that upon recognition of extracellular Glc6P UhpC induces auto-phosphorylation of UhpB.…”

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confidence: 99%

“…Although it has previously been speculated that transport of Glc6P by UhpC is not necessary to induce the expression of uhpT (15), it is of general biological interest to verify whether UhpC is able to transport Glc6P (as we claim for HPTcp) and to characterize its basic biochemical properties. Moreover, from the point of view of human infections caused by various chlamydial species it is of interest to study the biochemical properties of transport proteins involved in the metabolism of the intracellular pathogen.…”

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confidence: 99%

“…Escherichia coli transports glucose-6-phosphate (Glc6P) via an inducible transport protein named UhpT that is part of the genomic locus uhp which encodes UhpT (the Glc6P transport protein), UhpB (the membrane-bound sensor kinase/phosphatase), UhpA (a soluble signal transduction component) and UhpC (the sensor for the presence of extracellular Glc6P) (15). UhpT is a typical member of the major facilitator superfamily (MFS) that is predicted to have 12 ␣-helical transmembrane domains (17).…”

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confidence: 99%

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Properties of the Glucose-6-Phosphate Transporter from Chlamydia pneumoniae (HPTcp) and the Glucose-6-Phosphate Sensor from Escherichia coli (UhpC)

2002

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The amino acid sequence of the proposed glucose-6-phosphate (Glc6P) transporter from Chlamydia pneumoniae (HPTcp; hexose phosphate transporter [Chlamydia pneumoniae]) exhibits a higher degree of similarity to the Escherichia coli Glc6P sensor (UhpC) than to the E. coli Glc6P transporter (UhpT). Overexpression of His-UhpC in a UhpT-deficient E. coli strain revealed that the sensor protein is also able to transport Glc6P and exhibits an apparent K m (Glc6P) of 25 M, whereas His-HPTcp exhibits an apparent K m (Glc6P) of 98 M. His-HPTcp showed a four-times-lower specific activity than His-UhpT but a 56-times-higher specific activity than His-UhpC. Like His-UhpT and His-UhpC, the carrier His-HPTcp performs a sugar-phosphate/inorganicphosphate antiporter mode of transport. Surprisingly, while physiological concentrations of inorganic phosphate competitively inhibited transport mediated by the E. coli proteins His-UhpT and His-UhpC, transport mediated by His-HPTcp was not inhibited. Interestingly, C 3 -organophosphates stimulated His-HPTcp activity but not His-UhpT-or His-UhpC-catalyzed Glc6P transport. In contrast to His-UhpC, the His-HPTcp protein does not act as a Glc6P sensor in the uhp regulon.

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Section: Structural Characteristics Of Uhpc and Hptcpmentioning

confidence: 94%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Properties of the Glucose-6-Phosphate Transporter from Chlamydia pneumoniae (HPTcp) and the Glucose-6-Phosphate Sensor from Escherichia coli (UhpC)

2002

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“…Two other proteins of the sugar transport family, namely, the Rco3 regulator of conidiation in Neurospora crassa (58) and the Mst1 protein from the ectomycorrhiza Amita muscaria (64), may also serve as glucose sensors. Similarly, the uhpC gene of Escherichia coli encodes a protein highly similar in sequence to UhpT, a permease for several organophosphate compounds including glucose-6-phosphate (47). The UhpC protein seems unable to mediate uptake of glucose-6-phosphate and is involved, rather, in transcriptional induction of the uhpT permease gene in response to micromolar levels of external glucose-6-phosphate (48).…”

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confidence: 99%

Amino Acid Signaling in Saccharomyces cerevisiae: a Permease-Like Sensor of External Amino Acids and F-Box Protein Grr1p Are Required for Transcriptional Induction of the AGP1 Gene, Which Encodes a Broad-Specificity Amino Acid Permease

Iraqui

Vissers

Bernard

et al. 1999

Molecular and Cellular Biology

245

308

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The SSY1 gene of Saccharomyces cerevisiae encodes a member of a large family of amino acid permeases. Compared to the 17 other proteins of this family, however, Ssy1p displays unusual structural features reminiscent of those distinguishing the Snf3p and Rgt2p glucose sensors from the other proteins of the sugar transporter family. We show here that SSY1 is required for transcriptional induction, in response to multiple amino acids, of the AGP1 gene encoding a low-affinity, broad-specificity amino acid permease. Total noninduction of the AGP1 gene in the ssy1⌬ mutant is not due to impaired incorporation of inducing amino acids. Conversely, AGP1 is strongly induced by tryptophan in a mutant strain largely deficient in tryptophan uptake, but it remains unexpressed in a mutant that accumulates high levels of tryptophan endogenously. Induction of AGP1 requires Uga35p(Dal81p/DurLp), a transcription factor of the Cys 6 -Zn 2 family previously shown to participate in several nitrogen induction pathways. Induction of AGP1 by amino acids also requires Grr1p, the F-box protein of the SCF Grr1 ubiquitin-protein ligase complex also required for transduction of the glucose signal generated by the Snf3p and Rgt2p glucose sensors. Systematic analysis of amino acid permease genes showed that Ssy1p is involved in transcriptional induction of at least five genes in addition to AGP1. Our results show that the amino acid permease homologue Ssy1p is a sensor of external amino acids, coupling availability of amino acids to transcriptional events. The essential role of Grr1p in this amino acid signaling pathway lends further support to the hypothesis that this protein participates in integrating nutrient availability with the cell cycle.

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Sensory Transport Proteins

Krämer

2009

Bacterial Signaling

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A transmembrane signalling complex controls transcription of the Uhp sugar phosphate transport system

Cited by 24 publications

References 20 publications

Properties of the Glucose-6-Phosphate Transporter from Chlamydia pneumoniae (HPTcp) and the Glucose-6-Phosphate Sensor from Escherichia coli (UhpC)

Properties of the Glucose-6-Phosphate Transporter from Chlamydia pneumoniae (HPTcp) and the Glucose-6-Phosphate Sensor from Escherichia coli (UhpC)

Amino Acid Signaling in Saccharomyces cerevisiae: a Permease-Like Sensor of External Amino Acids and F-Box Protein Grr1p Are Required for Transcriptional Induction of the AGP1 Gene, Which Encodes a Broad-Specificity Amino Acid Permease

Sensory Transport Proteins

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