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Direct interaction between a membrane domain subunit and a connector subunit in the H + ‐translocating NADH‐quinone oxidoreductase
Author(s) -
Di Bernardo Salvatore,
Yagi Takao
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03111-8
Subject(s) - paracoccus denitrificans , protein subunit , membrane , escherichia coli , biochemistry , chemistry , oxidoreductase , biology , enzyme , gene
When Paracoccus denitrificans membranes were treated with a crosslinker, m ‐maleimidobenzoyl‐ N ‐hydroxysuccinimide ester (MBS), a cross‐linked product of M r ∼31 kDa was found which reacted with antibodies against the hydrophobic subunit Nqo7 and the connector subunit Nqo6. NaI treatment of the Paracoccus membranes before, but not after, the crosslinking step prevented the formation of the 31 kDa band. When Nqo7 and Nqo6 were coexpressed in Escherichia coli , both subunits were located in the membrane fraction. MBS treatment of the E. coli membranes generated the 31 kDa band as in the Paracoccus membranes. These results indicate that Nqo7 interacts with probable N2‐binding Nqo6.