Abstract
A new gap junction gene isolated from the mouse genome codes for a connexin 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-26 (77% amino acid sequence identity). The coding region of mouse connexin-30 is uninterrupted by introns and is detected in the mouse genome as a single copy gene that is assigned to mouse chromosome 14 by analysis of mouse x hamster somatic cell hybrids. Abundant amounts of connexin-30 mRNA (two transcripts of 2.0 and 2.3 kilobase pairs) were found after 4 weeks of postnatal development in mouse brain and skin. Microinjection of connexin-30 cRNA into Xenopus oocytes induced formation of functional gap junction channels that gated somewhat asymmetrically in response 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-26 and connexin-32 produced channels with highly asymmetric and rectifying voltage gating, respectively. This suggests that the polarity of voltage gating and the cationic selectivity of connexin-30 are similar to those of its closest homologue, connexin-26.
Original language | English (US) |
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Pages (from-to) | 17903-17910 |
Number of pages | 8 |
Journal | Journal of Biological Chemistry |
Volume | 271 |
Issue number | 30 |
DOIs | |
State | Published - 1996 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Biochemistry
- Cell Biology