E. Dahl et al., MOLECULAR-CLONING AND FUNCTIONAL EXPRESSION OF MOUSE CONNEXIN-30, A GAP JUNCTION GENE HIGHLY EXPRESSED IN ADULT BRAIN AND SKIN, The Journal of biological chemistry, 271(30), 1996, pp. 17903-17910
A new gap junction gene isolated from the mouse genome codes for a con
nexin protein of 261 amino acids, Because of its theoretical molecular
mass of 30.366 kDa, it is named connexin-30. Within the connexin gene
family, this protein is most closely related to connexin-ae (77% amin
o acid sequence identity). The coding region of mouse connexin-30 is u
ninterrupted by introns and is detected in the mouse genome as a singl
e copy gene that is assigned to mouse chromosome 14 by analysis of mou
se x hamster somatic cell hybrids. Abundant amounts of connexin-30 mRN
A (two transcripts of 2.0 and 2.3 kilobase pairs) were found after 4 w
eeks of postnatal development in mouse brain and skin, Microinjection
of connexin-30 cRNA into Xenopus oocytes induced formation of function
al gap junction channels that gated somewhat asymmetrically in respons
e to transjunctional voltage and at significantly lower voltage (V-o =
+38 and -46 mV) than the closely homologous connexin-26 channels (V-o
= 89 mV). Heterotypic pairings of connexin-30 with connexin-as and co
nnexin-32 produced channels with highly asymmetric and rectifying volt
age gating, respectively. This suggests that the polarity of voltage g
ating and the cationic selectivity of connexin-30 are similar to those
of its closest homologue, connexin-26.