Molecular cloning and expression characterization of a rice K+ channel beta subunit.
K+ channel proteins native to animal membranes have been shown to be composed of two different types of polypeptides: the pore-forming alpha subunit and the beta subunit which may be involved in either modulation of conductance through the channel, or stabilization and surface expression of the channel complex. Several cDNAs encoding animal K+ channel beta subunits have been recently cloned and sequenced. We report the molecular cloning of a rice plant homolog of these animal beta subunits. The rice cDNA (KOB1) described in this report encodes a 36 kDa polypeptide which shares 45% sequence identity with these animal K+ channel beta subunits. and 72% identity with the only other cloned plant (Arabidopsis thaliana) K+ channel beta subunit (KAB1). The KOB1 translation product was demonstrated to form a tight physical association with a plant K+ channel alpha subunit. These results are consistent with the conclusion that the KOB1 cDNA encodes a K+ channel beta subunit. Expression studies indicated that KOB1 protein is more abundant in leaves than in either reproductive structures or roots. Later-developing leaves on a rice plant were found to contain increasing levels of the protein with the flag leaf having the highest titer of KOB1. Leaf sheaths are known to accumulate excess K+ and act as reserve sources of this cation when new growth requires remobilization of K+. Leaf sheaths were found to contain higher levels of KOB1 protein than the blade portions of leaves. It was further determined that when K+ was lost from older leaves of plants grown on K+-deficient fertilizer, the loss of cellular K+ was associated with a decline in both KOB1 mRNA and protein. This finding represents the first demonstration (in either plants or animals) that changes in cellular K+ status may specifically alter expression of a gene encoding a K+ channel subunit.
Plant Science Department, College of Agriculture and Natural Resources, University of Connecticut, Storrs 06269-4067, USA.
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Fang
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Kamasani
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Berkowitz
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics; D018744:DNA, Plant / Q000235:genetics; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D008969:Molecular Sequence Data; D012275:Oryza / Q000235:genetics* / Q000378:metabolism*; D015221:Potassium Channels / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D018749:RNA, Plant / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D018076:DNA, Complementary; D018744:DNA, Plant; D015221:Potassium Channels; D012333:RNA, Messenger; D018749:RNA, Plant