A leucine motif in the amino acid sequence of subunit 9 of the mitochondrial ATPase, and other hydrophobic membrane proteins, that is highly conserved by editing.
Subunit 9 of the mitochondrial ATPase, but also other hydrophobic mitochondrially encoded proteins, contains a high frequency of the leucine motif, -Leu-X9-Leu-, which is highly conserved through RNA editing. The leucine motif may provide specific recognition sites between membrane-spanning domains of the F0-ATPase and between other hydrophobic subunits during the assembly of multienzyme complexes in the inner mitochondrial membrane.
Laboratory of Plant Genetic Engineering, Siberian Institute of Plant Physiology and Biochemistry, Irkutsk, Russian Federation.
Y M
YM
Konstantinov
I M
IM
Møller
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D017124:Conserved Sequence; D007930:Leucine; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D017393:RNA Editing; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013025:Glycine max / Q000201:enzymology; D014908:Triticum / Q000201:enzymology
D006180:Proton-Translocating ATPases; D007930:Leucine