Identification of a residue in the translocation pathway of a membrane carrier

Run Tao Yan, Peter C. Maloney

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)37-44
Number of pages8
JournalCell
Volume75
Issue number1
StatePublished - Oct 8 1993

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Glucose-6-Phosphate
Membranes
Cysteine
Antiporters
Mutagenesis
Escherichia coli
Cytoplasm
Substrates

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Yan, R. T., & Maloney, P. C. (1993). Identification of a residue in the translocation pathway of a membrane carrier. Cell, 75(1), 37-44.

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 journalArticle

Yan, RT & Maloney, PC 1993, 'Identification of a residue in the translocation pathway of a membrane carrier', Cell, vol. 75, no. 1, pp. 37-44.
Yan, Run Tao ; Maloney, Peter C. / Identification of a residue in the translocation pathway of a membrane carrier. In: Cell. 1993 ; Vol. 75, No. 1. pp. 37-44.
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