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Biophys J, August 1999, p. 775-788, Vol. 77, No. 2
*Laboratory of Experimental and Computational Biology, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5677 USA; #Laboratory of Membrane Biochemistry, Faculty of Pharmaceutical Sciences, Chiba University, Inage-ku, Chiba 263, Japan; and §Abteilung Mikrobiologie, Universität Osnabrück, D-49069 Osnabrück, Germany
The hypothesis is presented that at least four families
of putative K+ symporter proteins, Trk and KtrAB from
prokaryotes, Trk1,2 from fungi, and HKT1 from wheat, evolved from
bacterial K+ channel proteins. Details of this hypothesis
are organized around the recently determined crystal structure of a
bacterial K+ channel: i.e., KcsA from Streptomyces
lividans. Each of the four identical subunits of this channel
has two fully transmembrane helices (designated M1 and M2), plus an
intervening hairpin segment that determines the ion selectivity
(designated P). The symporter sequences appear to contain four
sequential M1-P-M2 motifs (MPM), which are likely to have arisen from
gene duplication and fusion of the single MPM motif of a bacterial
K+ channel subunit. The homology of MPM motifs is supported
by a statistical comparison of the numerical profiles derived from multiple sequence alignments formed for each protein family.
Furthermore, these quantitative results indicate that the KtrAB family
of symporters has remained closest to the single-MPM ancestor protein.
Strong sequence evidence is also found for homology between the
cytoplasmic C-terminus of numerous bacterial K+ channels
and the cytoplasm-resident TrkA and KtrA subunits of the Trk and KtrAB
symporters, which in turn are homologous to known dinucleotide-binding
domains of other proteins. The case for homology between bacterial
K+ channels and the four families of K+
symporters is further supported by the accompanying manuscript, in
which the patterns of residue conservation are demonstrated to be
similar to each other and consistent with the known 3D structure of the
KcsA K+ channel.
Biophys J, August 1999, p. 775-788, Vol. 77, No. 2
© 1999 by the Biophysical Society 0006-3495/99/08/775/14 $2.00
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