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.
Konstantinov
Y M
YM
Laboratory of Plant Genetic Engineering, Siberian Institute of Plant Physiology and Biochemistry, Irkutsk, Russian Federation.
Møller
I M
IM
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