A family of putative chloride channels from Arabidopsis and functional complementation of a yeast strain with a CLC gene disruption

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Item Type:	Article
Title:	A family of putative chloride channels from Arabidopsis and functional complementation of a yeast strain with a CLC gene disruption
Creators Name:	Hechenberger, M., Schwappach, B., Fischer, W.N., Frommer, W.B., Jentsch, T.J. and Steinmeyer, K.
Abstract:	We have cloned four novel members of the CLC family of chloride channels from Arabidopsis thaliana. The four plant genes are homologous to a recently isolated chloride channel gene from tobacco (CLC-Nt1; Lurin, C., Geelen, D., Barbier-Brygoo, H., Guern, J., and Maurel, C. (1996) Plant Cell 8, 701-711) and are about 30% identical in sequence to the most closely related CLC-6 and CLC-7 putative chloride channels from mammalia. AtCLC transcripts are broadly expressed in the plant. Similarly, antibodies against the AtCLC-d protein detected the protein in all tissues, but predominantly in the silique. AtCLC-a and AtCLC-b are highly homologous to each other ( approximately 87% identity), while being approximately 50% identical to either AtCLC-c or AtCLC-d. None of the four cDNAs elicited chloride currents when expressed in Xenopus oocytes, either singly or in combination. Among these genes, only AtCLC-d could functionally substitute for the single yeast CLC protein, restoring iron-limited growth of a strain disrupted for this gene. Introduction of disease causing mutations, identified in human CLC genes, abolished this capacity. Consistent with a similar function of both proteins, the green fluorescent protein-tagged AtCLC-d protein showed the identical localization pattern as the yeast ScCLC protein. This suggests that in Arabidopsis AtCLC-d functions as an intracellular chloride channel.
Keywords:	Amino Acid Sequence, Arabidopsis, Chloride Channels, Consensus Sequence, Complementary DNA, Plant DNA, Plant Genes, Genetic Complementation Test, Molecular Sequence Data, Muscle Proteins, Polymerase Chain Reaction, Transfection, Animals, Xenopus Laevis
Source:	Journal of Biological Chemistry
ISSN:	0021-9258
Publisher:	American Society for Biochemistry and Molecular Biology
Volume:	271
Number:	52
Page Range:	33632-33638
Date:	27 December 1996
Official Publication:	https://doi.org/10.1074/jbc.271.52.33632
PubMed:	View item in PubMed

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