Transmembrane Topology of Subunit N of Complex I (NADH:ubiquinone Oxidoreductase) from Escherichia Coli
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Biology
Endocrinology
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The transmembrane topology of subunit N from E. coli Complex I has been investigated. Chemical labeling of mono-substituted cysteine mutants was carried out in inverted membrane vesicles, and in whole cells, using 3-N-maleimidyl-propionyl biocytin (MPB). The results support a model of 14 transmembrane spans with both termini in the periplasm, and are consistent with the models of subunits L, M and N from the crystal structure of the membrane arm of the E. coli Complex I (Efremov et al. (2010) Nature 465, 441-445). In particular, the results do not support an unusual cytoplasmic localization of two likely transmembrane regions, as proposed in previous studies (Mathiesen and Hägerhäll (2002) Biochim Biophys Acta 1556, 121-132; Torres-Bacete, et al. (2009) J Biol Chem 284, 33062-33069).
Morino M, Ogoda S, Krulwich T, Ito M Extremophiles. 2016; 21(1):51-64.
PMID: 27709304 DOI: 10.1007/s00792-016-0877-z.
Michel J, DeLeon-Rangel J, Zhu S, Van Ree K, Vik S PLoS One. 2011; 6(2):e17420.
PMID: 21387012 PMC: 3046159. DOI: 10.1371/journal.pone.0017420.