Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/3902
Título: Yeast water channels: an overview of orthodox aquaporins
Autor: Soveral, Graça
Prista, Catarina
Moura, Teresa F.
Loureiro-Dias, Maria C.
Palavras-chave: Aquaporins
Genome sequence
Water transport
Data: 2011
Editora: Portland Press
Citação: Biology of the Cell (2011) 103, (35–54)
Resumo: In yeasts, the presence of orthodox aquaporins has been first recognized in Saccharomyces cerevisiae, in which two genes (AQY1 and AQY2) were shown to be related to mammal and plant water channels. The present review summarizes the putative orthodox aquaporin protein sequences found in available genomes of yeast and filamentous fungi. Among the 28 yeast genomes sequenced, most species present only one orthodox aquaporin and no aquaporins were found in 8 yeast species. Alignment of amino acid sequences reveals a very diverse group. Similarity values vary from 99% among species within the Saccharomyces genus to 34% between ScAqy1 and the aquaporin from Debaryomyces hansenii. All the fungal aquaporins possess the known characteristic sequences, and residues involved in the water channel pore are highly conserved. Advances in the establishment of the structure are reviewed in relation with the mechanisms of selectivity, conductance and gating. In particular, the involvement of the protein cytosolic N-terminal as a channel blocker preventing water flow is addressed. Methodologies used in the evaluation of aquaporin activity frequently involve the measurement of fast volume changes. Particular attention is paid to data analysis to obtain accurate membrane water permeability parameters. Although the presence of aquaporins clearly enhances membrane water permeability, the relevance of these ubiquitous water channels in yeast performance remains obscure.
Descrição: The final version of record is available at http://www.biolcell.org/boc/103/boc1030035.htm. A versão final do registo está disponível em http://www.biolcell.org/boc/103/boc1030035.htm.
Peer review: yes
URI: http://dx.doi.org/10.1042/BC20100102
ISSN: 0248-4900
Versão do Editor: http://www.biolcell.org/boc/103/boc1030035.htm
Aparece nas colecções:FF - Artigos em Revistas Internacionais

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