Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes

Abstract 

The large membrane protein complexes of mitochondrial oxidative phosphorylation are composed of central subunits that are essential for their bioenergetic core function and accessory subunits that may assist in regulation, assembly or stabilization. Although sequence conservation is low, a significant proportion of the accessory subunits is characterized by a common single transmembrane (STMD) topology. The STMD signature is also found in subunits of other membrane protein complexes. We hypothesize that the general function of STMD subunits is to organize the hydrophobic subunits of large membrane protein complexes in specialized environments like the inner mitochondrial membrane.

Abbreviations: LILBID, laser induced liquid bead ion desorption, LMW subunit, low molecular weight subunit, MALDI, matrix assisted laser desorption ionisation, STMD, single transmembrane domain, OXPHOS, oxidative phosphorylation

Keywords: Accessory subunit, Assembly, Membrane protein, Mitochondria, Oxidative phosphorylation, Photosystem