Abstract
Preliminary work using directed mutagenesis proved that cysteine is not required for operation of UhpT, the anion exchange protein responsible for glucose 6-phosphate transport by E. coli. We then made a detailed study of C143 and C265, because these cysteines impart sensitivity to p-chloromercuribenzosulfonate (PCMBS), a sulfhydral agent resembling glucose 6-phosphate in size, shape, and charge. We showed that C143 was exposed to the cytoplasm, as expected from hydropathy analysis, but we found no sidedness for C265. Rather, C265 was accessible to PCMBS from both membrane surfaces. And since the attack at C265 was blocked by glucose 6-phosphate, position 265 must lie directly on the pathway taken by the substrate as it moves through this membrane carrier.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 37-44 |
| Number of pages | 8 |
| Journal | Cell |
| Volume | 75 |
| Issue number | 1 |
| State | Published - Oct 8 1993 |
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ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Cite this
Identification of a residue in the translocation pathway of a membrane carrier. / Yan, Run Tao; Maloney, Peter C.
In: Cell, Vol. 75, No. 1, 08.10.1993, p. 37-44.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of a residue in the translocation pathway of a membrane carrier
AU - Yan, Run Tao
AU - Maloney, Peter C.
PY - 1993/10/8
Y1 - 1993/10/8
N2 - Preliminary work using directed mutagenesis proved that cysteine is not required for operation of UhpT, the anion exchange protein responsible for glucose 6-phosphate transport by E. coli. We then made a detailed study of C143 and C265, because these cysteines impart sensitivity to p-chloromercuribenzosulfonate (PCMBS), a sulfhydral agent resembling glucose 6-phosphate in size, shape, and charge. We showed that C143 was exposed to the cytoplasm, as expected from hydropathy analysis, but we found no sidedness for C265. Rather, C265 was accessible to PCMBS from both membrane surfaces. And since the attack at C265 was blocked by glucose 6-phosphate, position 265 must lie directly on the pathway taken by the substrate as it moves through this membrane carrier.
AB - Preliminary work using directed mutagenesis proved that cysteine is not required for operation of UhpT, the anion exchange protein responsible for glucose 6-phosphate transport by E. coli. We then made a detailed study of C143 and C265, because these cysteines impart sensitivity to p-chloromercuribenzosulfonate (PCMBS), a sulfhydral agent resembling glucose 6-phosphate in size, shape, and charge. We showed that C143 was exposed to the cytoplasm, as expected from hydropathy analysis, but we found no sidedness for C265. Rather, C265 was accessible to PCMBS from both membrane surfaces. And since the attack at C265 was blocked by glucose 6-phosphate, position 265 must lie directly on the pathway taken by the substrate as it moves through this membrane carrier.
UR - http://www.scopus.com/inward/record.url?scp=0027484363&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027484363&partnerID=8YFLogxK
M3 - Article
C2 - 8402899
AN - SCOPUS:0027484363
VL - 75
SP - 37
EP - 44
JO - Cell
JF - Cell
SN - 0092-8674
IS - 1
ER -