Key result
Deletion of the 14 N-terminal amino acids of the Kcv channel abolishes measurable current in transfected cells without affecting protein expression or subcellular location.
The short N-terminus of the virus-encoded miniature K+ channel Kcv is essential for its functional properties but not for protein expression.
N-terminus essential for Kcv function in vitro; hypothesis-generating for channel gating, requires native system validation.
Kcv (K(+) Chlorella virus) is a miniature virus-encoded K(+) channel. Its predicted membrane-pore-membrane structure lacks a cytoplasmic C-terminus and it has a short 12 amino acid (aa) cytoplasmic N-terminus. Kcv forms a functional channel when expressed in human HEK 293 cells. Deletion of the 14 N-terminal aa results in no apparent differences in the subcellular location and expression level of the Kcv protein. However, the truncated protein does not induce a measurable current in transfected HEK 293 cells or Xenopus oocytes. We conclude that the N-terminus controls functional properties of the Kcv channel, but does not influence protein expression.
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Moroni et al. (2002) studied this question. Deletion of the 14 N-terminal amino acids of Kcv vs. Wild-type Kcv was evaluated on Measurable current in transfected cells. Deletion of the 14 N-terminal amino acids of the Kcv channel abolishes measurable current in transfected cells without affecting protein expression or subcellular location.
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