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Chlorella virus ATCV-1 encodes a functional potassium channel of 82 amino acids.

Gazzarrini, Sabrina ; Kang, Ming ; Abenavoli, Alessandra ; Romani, Giulia ; Olivari, Claudio ; Gaslini, Daniele ; Ferrara, Giuseppina ; Etten, James L. van ; Kreim, Michael ; Kast, Stefan M. ; Thiel, Gerhard ; Moroni, Anna (2009)
Chlorella virus ATCV-1 encodes a functional potassium channel of 82 amino acids.
In: The Biochemical journal, 420 (2)
Article, Bibliographie

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.

Item Type: Article
Erschienen: 2009
Creators: Gazzarrini, Sabrina ; Kang, Ming ; Abenavoli, Alessandra ; Romani, Giulia ; Olivari, Claudio ; Gaslini, Daniele ; Ferrara, Giuseppina ; Etten, James L. van ; Kreim, Michael ; Kast, Stefan M. ; Thiel, Gerhard ; Moroni, Anna
Type of entry: Bibliographie
Title: Chlorella virus ATCV-1 encodes a functional potassium channel of 82 amino acids.
Language: English
Date: 2009
Journal or Publication Title: The Biochemical journal
Volume of the journal: 420
Issue Number: 2
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.

Divisions: 10 Department of Biology
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10 Department of Biology > Plant Membrane Biophyscis (20.12.23 renamed in Biology of Algae and Protozoa)
Date Deposited: 21 Jun 2011 12:06
Last Modified: 20 Aug 2021 09:43
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