What we can learn from the effects of thiol reagents on transport proteins
- PMID: 1510995
- DOI: 10.1016/0304-4157(92)90037-b
What we can learn from the effects of thiol reagents on transport proteins
Abstract
Many secondary membrane transport systems contain reactive sulfhydryl groups. In this review the applications of SH reagents for analyzing the role of sulfhydryl groups in membrane transport systems will be discussed. First an overview will be given of the more important reagents, that have been used to study SH-groups in membrane transport systems, and examples will be given of transport proteins in which the role of cysteines have been analyzed. An important application of SH-reagents to label transport proteins using various SH-reagents modified with fluorescent- or spin-label moieties will be discussed. Two general models are shown which have been proposed to explain the role of sulfhydryl groups in some membrane transport systems.
Similar articles
-
Identification of the amine-polyamine-choline transporter superfamily 'consensus amphipathic region' as the target for inactivation of the Escherichia coli GABA transporter GabP by thiol modification reagents. Role of Cys-300 in restoring thiol sensitivity to Gabp lacking Cys.Biochem J. 1999 May 1;339 ( Pt 3)(Pt 3):649-55. doi: 10.1042/bj3390649. Biochem J. 1999. PMID: 10215604 Free PMC article.
-
The kamikaze approach to membrane transport.Nat Rev Mol Cell Biol. 2001 Aug;2(8):610-20. doi: 10.1038/35085077. Nat Rev Mol Cell Biol. 2001. PMID: 11483994 Review.
-
Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli.Proc Natl Acad Sci U S A. 2003 Sep 2;100(18):10187-92. doi: 10.1073/pnas.1434239100. Epub 2003 Aug 21. Proc Natl Acad Sci U S A. 2003. PMID: 12934015 Free PMC article.
-
Cysteine-scanning mutagenesis of helix VI and the flanking hydrophilic domains on the lactose permease of Escherichia coli.Biochemistry. 1996 Apr 23;35(16):5333-8. doi: 10.1021/bi953068d. Biochemistry. 1996. PMID: 8611521
-
The lactose permease of Escherichia coli: a paradigm for membrane transport proteins.Soc Gen Physiol Ser. 1993;48:1-9. Soc Gen Physiol Ser. 1993. PMID: 8503038 Review. No abstract available.
Cited by
-
Effectors of the mammalian plasma membrane NADH-oxidoreductase system. Short-chain ubiquinone analogues as potent stimulators.J Bioenerg Biomembr. 1996 Dec;28(6):531-40. doi: 10.1007/BF02110443. J Bioenerg Biomembr. 1996. PMID: 8953385
-
The role of cysteines and histidins of the norepinephrine transporter.Neurochem Res. 2013 Jul;38(7):1303-14. doi: 10.1007/s11064-013-1022-3. Epub 2013 Mar 23. Neurochem Res. 2013. PMID: 23525969
-
Modulation of DMT1 activity by redox compounds.J Membr Biol. 2004 Jan 15;197(2):91-9. doi: 10.1007/s00232-003-0644-9. J Membr Biol. 2004. PMID: 15014911
-
The increase in the number of accessible SH-groups in the enterococcal membrane vesicles by ATP and nicotinamide adenine dinucleotides.Curr Microbiol. 2006 Apr;52(4):300-4. doi: 10.1007/s00284-005-0293-6. Epub 2006 Mar 18. Curr Microbiol. 2006. PMID: 16550463
-
Dopamine inactivates tryptophan hydroxylase and forms a redox-cycling quinoprotein: possible endogenous toxin to serotonin neurons.J Neurosci. 1998 Sep 15;18(18):7111-7. doi: 10.1523/JNEUROSCI.18-18-07111.1998. J Neurosci. 1998. PMID: 9736634 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
