Abstract：
:Plant sucrose transporters (SUTs) are functional as sucrose-proton-cotransporters with an optimal transport activity in the acidic pH range. Recently, the pH optimum of the Solanum tuberosum sucrose transporter StSUT1 was experimentally determined to range at an unexpectedly low pH of 3 or even below. Various research groups have confirmed these surprising findings independently and in different organisms. Here we provide further experimental evidence for a pH optimum at physiological extrema. Site directed mutagenesis provides information about functional amino acids, which are highly conserved and responsible for this extraordinary increase in transport capacity under extreme pH conditions. Redox-dependent dimerization of the StSUT1 protein was described earlier. Here the ability of StSUT1 to form homodimers was demonstrated by heterologous expression in Lactococcus lactis and Xenopus leavis using Western blots, and in plants by bimolecular fluorescence complementation. Mutagenesis of highly conserved cysteine residues revealed their importance in protein stability. The accessibility of regulatory amino acid residues in the light of StSUT1's compartmentalization in membrane microdomains is discussed.
journal_name
Biochimiejournal_title
Biochimieauthors
Krügel U,Wiederhold E,Pustogowa J,Hackel A,Grimm B,Kühn Cdoi
10.1016/j.biochi.2013.07.028subject
Has Abstractpub_date
2013-11-01 00:00:00pages
2132-44issue
11eissn
0300-9084issn
1638-6183pii
S0300-9084(13)00251-4journal_volume
95pub_type
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