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Phylogenetic analysis of the domains that conform the NADPH oxidases
Author(s) -
JuliánSánchez Adriana,
MagisWeinberg Lucía,
RiverosRosas Héctor
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb161
Subject(s) - phylogenetic tree , in silico , phylogenetics , biology , flavin group , biochemistry , multiple sequence alignment , monophyly , reductase , sequence alignment , protein domain , genetics , computational biology , gene , enzyme , peptide sequence , clade
NADPH oxidases (Nox) are eukaryotic enzymes used deliberately to produce superoxide radicals. In a previous work (Mol. Microbiol (2003) 50: 1241), we show evidence that suggests that Nox evolutionarily derived from ferric reductases, which have been described in animals, plants, fungi and bacteria. Both are membrane proteins and contain a cytochrome b as well as flavin, and possess three different domains: a FAD binding domain, a NADP + binding domain, and a ferric reductase domain. In this work a phylogenetic independent analysis was made for each one of these domains, to obtain additional insight about the origin of Nox. The analysis was carried out in silico, starting from the protein sequences obtained on public databases (PFAM, NCBI and SwissProt), that possess the NADP + binding domain (565 sequences), FAD binding domain (607 sequences) and ferric reductase domain (1012 sequences). The domain alignments were built with Clustal_X (corrected manually with BLASP results). Phylogenetic analysis was performed in MEGA 4.0. The results show that in the three analyzed domain, all the Nox comprise a monophyletic group; however, its relationship with the ferric reductases (the proposed ancestral group) is not so clear when the domains in an independent way are analyzed. This contrast to the obtained results with the complete sequences. Supported partially by DGAPA‐UNAM grant IN208510‐3.