(
a) Comparison of
C. elegans (
C.e) CLHs, human (
H.s), and murine (
M.m) ClC-2. Amino acids altered in
clh-1(pe) alleles (deep and light blue) and their flanking regions are shown. The ‘Proton glutamate’ residue is boxed, which predicts whether the corresponding ClC protein is an anion channel or a H
+/Cl
- antiporter (
Accardi et al., 2005). Members that carry glutamate (
E) at the position is proposed as a H
+/Cl
- antiporter, whereas anion channel if it is valine (
V). Although CLH-1 and CLH-2 carry serine (
S) residue at this position, they are presumed to be anion channels because they share high similarity with mammalian ClC-2 (
Schriever et al., 1999;
Nehrke et al., 2000). (
b) Chemotaxis of the single deletion mutants of each ClC gene (
clh-1 through
clh-6). All mutant strains were outcrossed with wild type more than four times. Dots represent individual trials. Bars and the error bars represent mean +/- s.e.m.,
n ≧ 5 assays, compared with wild type, Dunnett’s test, ***p<0.001. (
c) Immobility index of the
clh deletion mutants. Dots represent individual trials. Bars and the error bars represent mean +/- s.e.m.,
n ≧ 5, compared with wild type, Dunnett’s test, ***p<0.001, **p<0.01. (
d) Immobility index of the
clh multiple mutants. Dots represent individual trials. Bars and the error bars represent mean +/- s.e.m.,
n ≧ 5, Tukey’s test, ***p<0.001, **p<0.01, *p<0.05, compared with wild type.