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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
Author(s) -
Konstantinov Yuri M.,
Møller Ian M.
Publication year - 1994
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 - 10.1016/0014-5793(94)01124-9
Subject(s) - protein subunit , inner mitochondrial membrane , leucine , biochemistry , mitochondrial carrier , atpase , biology , sequence motif , peptide sequence , amino acid , conserved sequence , mitochondrion , chemistry , microbiology and biotechnology , dna , enzyme , bacterial outer membrane , gene , escherichia coli
Subunit 9 of the mitochondrial ATPase, but also other hydrophobic mitochondrially encoded proteins, contains a high frequency of the leucine motif, ‐Leu‐X 9 ‐Leu‐, which is highly conserved through RNA editing. The leucine motif may provide specific recognition sites between membrane‐spanning domains of the F 0 ‐ATPase and between other hydrophobic subunits during the assembly of multienzyme complexes in the inner mitochondrial membrane.