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Diversity and evolution of eukaryotic NADPH oxidases
Author(s) -
JulianSanchez Adriana,
Magis Lucia,
Piña Enrique,
RiverosRosas Hector
Publication year - 2007
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.21.6.lb28-c
Subject(s) - p22phox , superoxide , nadph oxidase , biology , protein subunit , microbiology and biotechnology , nox , genetics , enzyme , biochemistry , chemistry , gene , reactive oxygen species , organic chemistry , combustion
NADPH oxidases (Nox) have been characterized as eukaryotic enzymes used deliberately to produce superoxide radicals. The recent discovery of new functional members of the Nox family in animals, plants, and fungi has lead to the recognition of the increasing importance of superoxide radicals as signaling molecules involved in the regulation of diverse cellular processes such as defense, proliferation, differentiation, apoptosis, and signal transduction. Inclusive, it has been proposed that the development of multicellular structures is related to the use of superoxide radicals as intercellular signaling. In a previous work, we performed a phylogenetic analysis of the gp91phox subunit of Nox (Lara‐Ortiz et al. (2003) Mol. Microbiol. 50: ) but a phylogenetic analysis of the other subunits that comprise this multisubunit oxidase is lacking. Therefore, the objective of this work was to analyze the diversity and evolution of the Nox complex, including besides the gp91phox, p22phox, p47phox, p67phox, p40phox, p42phox, p41 Nox, and P51Nox. Results show substantial differences between the phyletic distribution of regulatory subunits of Nox, which are completely absent in plants. In the same way, p22phox and p47phox are restricted to animals. Therefore, additional subunits to gp91phox are not essential to the enzyme function. Phylogenetic analysis suggests that Nox5 are the ancestral group inside this protein family. Supported by CONACYT‐México grant 45003M and DGAPA‐UNAM grant IN224206‐2.