ISSN:
1573-6881
Schlagwort(e):
Yeast
;
proton ATPase
;
sequence alignment
;
hydrophobic regions
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Chemie und Pharmazie
,
Physik
Notizen:
Abstract Seventeen protein sequences of H+-ATPases from plants (Arabidopsis thaliana, Nicotiana plumbaginifolia, Lycopersicum esculentum), fungi (Sacharomyces cerevisiae, Schizosaccharomyces pombe, Zygosaccharomyces rouxii, Neuropora crassa, Candida albicans), and a parasitic ciliate (Leishmania donovani) have been aligned. Twenty sequence fragments were identified which were conserved in H+-, Na+/K+-, and Ca++ plasma membrane-ATPases. In addition, a total of 118 residues not located in these fragments were found to be conserved in all H+-ATPases. Among those, 38 amino acid residues were screened out as being priority targets for site-directed mutagenesis experiments aimed at the identification of the amino acid residues specifically involved in cation specificity.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00768851
