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Chlorella virus ATCV1 encodes a functional potassium channel of eighty-two amino acids. (Articolo in rivista)

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Chlorella virus ATCV1 encodes a functional potassium channel of eighty-two amino acids. (Articolo in rivista) (literal)

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Gazzarrini S.; Kang M.; Abenavoli A.; Romani G.; Olivari C.; Gaslini D.; Ferrara G.; Van Etten J. L.; Kreim M.; Kast S.M.; Thiel G.; Moroni A. (2009)
Chlorella virus ATCV1 encodes a functional potassium channel of eighty-two amino acids.
in Biochemical journal (Lond., 1984)
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Gazzarrini S.; Kang M.; Abenavoli A.; Romani G.; Olivari C.; Gaslini D.; Ferrara G.; Van Etten J. L.; Kreim M.; Kast S.M.; Thiel G.; Moroni A. (literal)

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Romani, G., Moroni, A.: IBF CNR Milano; Gazzarrini, S., Abenavoli, A., Olivari, C., Gaslini, D., Ferrara, G., Moroni A.: Dipartimento di Biologia Univ. degli Studi Milano; Kang. M., Van Etten, J. L.: Department of Plant Pathology and Nebraska Center for Virology, University of Nebraska, Lincoln, NE 68583-0900, U.S.A.; Kast, S.M., Kreim, M.: Eduard-Zintl-Institut f¨ur Anorganische und Physikalische Chemie, Technische Universit¨at Darmstadt, Germany; Thiel, G.: Institute of Botany, Darmstadt University of Technology, Germany (literal)

Titolo

Chlorella virus ATCV1 encodes a functional potassium channel of eighty-two amino acids. (literal)

Abstract

Chlorella virus PBCV-1 (Paramecium bursaria chlorella virus-1) encodes the smallest protein (94 amino acids, named Kcv) previously known to form a functional K+ channel in heterologous systems. In this paper, we characterize another chlorella virus encoded K+ channel protein (82 amino acids, named ATCV-1 Kcv) that forms a functional channel in Xenopus oocytes and rescues Saccharomyces cerevisiae mutants that lack endogenous K+ uptake systems. Compared with the larger PBCV-1 Kcv, ATCV-1 Kcv lacks a cytoplasmic N-terminus and has a reduced number of charged amino acids in its turret domain. Despite these deficiencies, ATCV-1 Kcv accomplishes all the major features of K+ channels: it assembles into a tetramer, is K+ selective and is inhibited by the canonical K+ channel blockers, barium and caesium. Single channel analyses reveal a stochastic gating behaviour and a voltage-dependent conductance that resembles the macroscopic I/V relationship. One difference between PBCV-1 and ATCV-1 Kcv is that the latter is more permeable to K+ than Rb+. This difference is partially explained by the presence of a tyrosine residue in the selective filter of ATCV-1 Kcv, whereas PBCV-1 Kcv has a phenylalanine. Hence, ATCV-1 Kcv is the smallest protein to form a K+ channel and it will serve as a model for studying structure-function correlations inside the potassium channel pore. (literal)

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