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pH Sensitivity of the Glu-GABA Antiporter 1 G 300 GadC AdC 250 SIA 2onendmoM enoto bbl 200 ale biu A esnerdmaM lodd E 150 bo 100 50- met boA1A e dmo ll dimse sullo bne 6. alidigilodgd Hoo bns 5. 6. 8. pH sdi diw batar picy mc s s oidw.enistong onndmam lan eupnue buo no biqiloyla bns anisaoqooylg nutnoo nndmsM os thun ansbi lloo z 1 torli sa Substrate accumulation (nmol per mg protein)

pH Sensitivity of the Glu-GABA Antiporter 1 G 300 GadC AdC 250 SIA 2onendmoM enoto bbl 200 ale biu A esnerdmaM lodd E 150 bo 100 50- met boA1A e dmo ll dimse sullo bne 6. alidigilodgd Hoo bns 5. 6. 8. pH sdi diw batar picy mc s s oidw.enistong onndmam lan eupnue buo no biqiloyla bns anisaoqooylg nutnoo nndmsM os thun ansbi lloo z 1 torli sa Substrate accumulation (nmol per mg protein)

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Question 2 Interpreting data

id bgilodgodg How Hemorrhagic E. coli Resists the Acid Environment G 3001 pH Sensitivity of the Glu-GABA Antiporter of the Stomach Gadc Adc 250 Recent years have been marked by a series of food poisoning outbreaks involving hemorrhagic (producing internal bleeding) strains of the bacterium Escherichia coli (E. coli). Bacteria are often a source of food poisoning. typically milder infections caused by food-borne strepto- coccal bacteria. Less able to bear the extremely acidic conditions encountered by food in the human stomach (pH = 2), E. coli has not been as common a problem. The hemorrhagic strains of E. coli responsible for recent out- breaks seem to have evolved more elaborate acid-resistance bne SIA 2ordmoM enioto bsbl long 200- biul A esnerdmaM lasio id iod g lode el bm Ini bnoo o labon in ors l n 150- eale 100- 50 4 met bdmeA A e dmo ull systems. pH onsini oefT em How do hemorrhagic E. coli bacteria survive in the acid environment of the stomach? The problem they face, in essence, is that they are submerged in a sea of hydrogen ions, many of which diffuse into their cells, To rid them-n Analysis selves of these excess hydrogen ions, the E. coli cells use aom clever system to pump hydrogen ions back out of their diw bateiso oidw.eniotong onandmom leginog no abiqilooyla bnu anisionqooyly nisinoo onndmsM.onsiT hum vioobi lloo 1s turli so dt 1. Applying Concepts ivo19 ebiqiloriqeor19 sa T9a a. Variable. In the graph, what is the dependento Isuount varjable? 6. Substrate. What is a substrate? In this ella biqil erlT L investigation, what are the substrates that are accumulating? c. pH. What is the difference in hydrogen vaws insino v ion concentration between pH 5 and pH 7?o ToiToini onuon How many times more (or less) is that? Explain.w b v 2. Interpreting Data a. Does the amount of amino acid transported ogitnos d in the 10-minute experimental intervalullib nes (expressed as substrate accumulation) vary l ordi no a with pH for the arginine-transporting AdiC l bancy antiporter? For the glutamate-transporting u GadC antiporter? b. Compare the amount of substrate accumulated by AdiC in 10 minutes at pH 9.0 with that otni to on accumulated at pH 5.0. What fraction of the low pH activity is observed at the higher pH? c. In a similar fashion, compare the amount ofnd substrate accumulated by GadC at pH 9.0 with that accumulated at pH 5.0. Whatm Issimsda fraction of the low pH activity is observed at m vn the higher pH? cells. First, the hemorrhagic E. coli cells take up cellulareM rh no hydrogen ions by using the enzyme glutamic acid decarbox- ylase (GAD) to convert the amino acid glutamate toA.2 owi lo bozog o Y-aminobutyric acid (GABA), a decarboxylation reaction thatlo2 uloa sinotozi Toyly node Vul odiailidqoid br consumes a hydrogen ion. iduloa Second, the hemorrhagic E. coli export this GABA 52ol from their cell cytoplasm using a Glu-GABA antiporter called GadC (this transmembrane protein channel is called an antiporter because it transports two molecules across the odi zqosd 1atew lo gnibnod nogoiby membrane in opposite directions). eviDA However, to survive elsewhere in the human body, it pe is important that the Glu-GABA antiporter of hemorrhagica E. coli not function, lest it short-circuit metabolism. To see if the GadC antiporter indeed functions only in acid environ-o ments, investigators compared its activity at a variety of pHsno with that of a different amino acid antiporter called AdiC,ob which transports arginine out of cells under a broad b range of conditions. The results of monitoring transport for dmsM 10 minutes are presented in the graph. oM of anolbmo nol aseU hoqansiT belquo) s2.e anolbeD noiterineono ioriT JenispA eolusoloM Outside ising olesba lloo-o-lls)is Otomib ati o aloslom 3. Making Inferences Would you say that the GadCion ibInside cell naibeg cell antiporter exhibits the same pH dependence as the al AdiC antiporter? If not, which antiporter is lessomansYT active at nonacid pHs? 4. Drawing Conclusions Is the glutamate-GABA antiporter GadC active at nonacid pHs? menYT igil GABA 29bizeniriiW 2922900 ons alaotyaob ta.a m liso sli ipobro ni 5. Further Analysis The GadC antiporter also o quiry & Analysis uoneinunppe ajegsgns (nmol per mg protein)
Transcribed Image Text:id bgilodgodg How Hemorrhagic E. coli Resists the Acid Environment G 3001 pH Sensitivity of the Glu-GABA Antiporter of the Stomach Gadc Adc 250 Recent years have been marked by a series of food poisoning outbreaks involving hemorrhagic (producing internal bleeding) strains of the bacterium Escherichia coli (E. coli). Bacteria are often a source of food poisoning. typically milder infections caused by food-borne strepto- coccal bacteria. Less able to bear the extremely acidic conditions encountered by food in the human stomach (pH = 2), E. coli has not been as common a problem. The hemorrhagic strains of E. coli responsible for recent out- breaks seem to have evolved more elaborate acid-resistance bne SIA 2ordmoM enioto bsbl long 200- biul A esnerdmaM lasio id iod g lode el bm Ini bnoo o labon in ors l n 150- eale 100- 50 4 met bdmeA A e dmo ull systems. pH onsini oefT em How do hemorrhagic E. coli bacteria survive in the acid environment of the stomach? The problem they face, in essence, is that they are submerged in a sea of hydrogen ions, many of which diffuse into their cells, To rid them-n Analysis selves of these excess hydrogen ions, the E. coli cells use aom clever system to pump hydrogen ions back out of their diw bateiso oidw.eniotong onandmom leginog no abiqilooyla bnu anisionqooyly nisinoo onndmsM.onsiT hum vioobi lloo 1s turli so dt 1. Applying Concepts ivo19 ebiqiloriqeor19 sa T9a a. Variable. In the graph, what is the dependento Isuount varjable? 6. Substrate. What is a substrate? In this ella biqil erlT L investigation, what are the substrates that are accumulating? c. pH. What is the difference in hydrogen vaws insino v ion concentration between pH 5 and pH 7?o ToiToini onuon How many times more (or less) is that? Explain.w b v 2. Interpreting Data a. Does the amount of amino acid transported ogitnos d in the 10-minute experimental intervalullib nes (expressed as substrate accumulation) vary l ordi no a with pH for the arginine-transporting AdiC l bancy antiporter? For the glutamate-transporting u GadC antiporter? b. Compare the amount of substrate accumulated by AdiC in 10 minutes at pH 9.0 with that otni to on accumulated at pH 5.0. What fraction of the low pH activity is observed at the higher pH? c. In a similar fashion, compare the amount ofnd substrate accumulated by GadC at pH 9.0 with that accumulated at pH 5.0. Whatm Issimsda fraction of the low pH activity is observed at m vn the higher pH? cells. First, the hemorrhagic E. coli cells take up cellulareM rh no hydrogen ions by using the enzyme glutamic acid decarbox- ylase (GAD) to convert the amino acid glutamate toA.2 owi lo bozog o Y-aminobutyric acid (GABA), a decarboxylation reaction thatlo2 uloa sinotozi Toyly node Vul odiailidqoid br consumes a hydrogen ion. iduloa Second, the hemorrhagic E. coli export this GABA 52ol from their cell cytoplasm using a Glu-GABA antiporter called GadC (this transmembrane protein channel is called an antiporter because it transports two molecules across the odi zqosd 1atew lo gnibnod nogoiby membrane in opposite directions). eviDA However, to survive elsewhere in the human body, it pe is important that the Glu-GABA antiporter of hemorrhagica E. coli not function, lest it short-circuit metabolism. To see if the GadC antiporter indeed functions only in acid environ-o ments, investigators compared its activity at a variety of pHsno with that of a different amino acid antiporter called AdiC,ob which transports arginine out of cells under a broad b range of conditions. The results of monitoring transport for dmsM 10 minutes are presented in the graph. oM of anolbmo nol aseU hoqansiT belquo) s2.e anolbeD noiterineono ioriT JenispA eolusoloM Outside ising olesba lloo-o-lls)is Otomib ati o aloslom 3. Making Inferences Would you say that the GadCion ibInside cell naibeg cell antiporter exhibits the same pH dependence as the al AdiC antiporter? If not, which antiporter is lessomansYT active at nonacid pHs? 4. Drawing Conclusions Is the glutamate-GABA antiporter GadC active at nonacid pHs? menYT igil GABA 29bizeniriiW 2922900 ons alaotyaob ta.a m liso sli ipobro ni 5. Further Analysis The GadC antiporter also o quiry & Analysis uoneinunppe ajegsgns (nmol per mg protein)
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