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Functional interactions between the subunits of the lactose transporter from Streptococcus thermophilus.

Abstract：

:Although the quaternary state has been assessed in detail for only a few members of the major facilitator superfamily (MFS), it is clear that multiple oligomeric states are represented within the MFS. One of its members, the lactose transporter LacS from Streptococcus thermophilus assumes a dimeric structure in the membrane and in vitro analysis showed functional interactions between both subunits when proton motive force ((Delta)p)-driven transport was assayed. To study the interactions in further detail, a covalent dimer was constructed consisting of in tandem fused LacS subunits. These covalent dimers, composed of active and completely inactive subunits, were expressed in Escherichia coli, and initial rates of (Delta)p-driven lactose uptake and lactose counterflow were determined. We now show that also in vivo, both subunits interact functionally; that is, partial complementation of the inactive subunit was observed for both transport modes. Thus, both subunits interact functionally in (Delta)p-driven uptake and in counterflow transport. In addition, analysis of in tandem fused LacS subunits containing one regulatory LacS-IIA domain showed that regulation is primarily an intramolecular event.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Geertsma ER,Duurkens RH,Poolman B

doi

10.1016/j.jmb.2005.04.047

keywords:

subject

Has Abstract

pub_date

2005-07-01 00:00:00

pages

102-11

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)00481-X

journal_volume

350

pub_type

杂志文章

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