Revised transmembrane orientation of the NADH:quinone oxidoreductase subunit NuoA.

Research output: Contribution to journalArticle

Standard

Revised transmembrane orientation of the NADH:quinone oxidoreductase subunit NuoA. / Virzintiene, Egle; Trane, Maria; Hägerhäll, Cecilia.

In: FEBS Letters, Vol. 585, 2011, p. 3277-3283.

Research output: Contribution to journalArticle

Harvard

APA

CBE

MLA

Vancouver

Author

Virzintiene, Egle ; Trane, Maria ; Hägerhäll, Cecilia. / Revised transmembrane orientation of the NADH:quinone oxidoreductase subunit NuoA. In: FEBS Letters. 2011 ; Vol. 585. pp. 3277-3283.

RIS

TY - JOUR

T1 - Revised transmembrane orientation of the NADH:quinone oxidoreductase subunit NuoA.

AU - Virzintiene, Egle

AU - Trane, Maria

AU - Hägerhäll, Cecilia

PY - 2011

Y1 - 2011

N2 - NuoA is a small membrane spanning subunit of respiratory chain NADH:quinone oxidoreductase (complex I). Unlike the other complex I core protein subunits, the NuoA protein has no known homologue in other enzyme systems. The transmembrane orientation of NuoA cannot be unambiguously predicted, due to the small size of the polypeptide and the varying distribution of charged amino acid residues in NuoA from different organisms. Novel analyses of NuoA from Escherichia coli complex I expressed as fusion proteins to cytochrome c and to alkaline phosphatase demonstrated that the c-terminal end of the polypeptide is localized in the bacterial cytoplasm, in contrast to what was previously reported for the homologous NQO7 subunit from Paracoccus denitrificans complex I.

AB - NuoA is a small membrane spanning subunit of respiratory chain NADH:quinone oxidoreductase (complex I). Unlike the other complex I core protein subunits, the NuoA protein has no known homologue in other enzyme systems. The transmembrane orientation of NuoA cannot be unambiguously predicted, due to the small size of the polypeptide and the varying distribution of charged amino acid residues in NuoA from different organisms. Novel analyses of NuoA from Escherichia coli complex I expressed as fusion proteins to cytochrome c and to alkaline phosphatase demonstrated that the c-terminal end of the polypeptide is localized in the bacterial cytoplasm, in contrast to what was previously reported for the homologous NQO7 subunit from Paracoccus denitrificans complex I.

U2 - 10.1016/j.febslet.2011.09.006

DO - 10.1016/j.febslet.2011.09.006

M3 - Article

VL - 585

SP - 3277

EP - 3283

JO - FEBS Letters

T2 - FEBS Letters

JF - FEBS Letters

SN - 1873-3468

ER -