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Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes
Author(s) -
Zickermann Volker,
Angerer Heike,
Ding Martina G.,
Nübel Esther,
Brandt Ulrich
Publication year - 2010
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/j.febslet.2010.04.021
Subject(s) - protein subunit , transmembrane protein , transmembrane domain , chemistry , inner mitochondrial membrane , membrane protein , function (biology) , microbiology and biotechnology , membrane , biochemistry , biology , gene , receptor
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.