Literature DB >> 7957931

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.

Y M Konstantinov1, I M Møller.   

Abstract

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.

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Year:  1994        PMID: 7957931     DOI: 10.1016/0014-5793(94)01124-9

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  Ca2+ binding to F-ATP synthase β subunit triggers the mitochondrial permeability transition.

Authors:  Valentina Giorgio; Victoria Burchell; Marco Schiavone; Claudio Bassot; Giovanni Minervini; Valeria Petronilli; Francesco Argenton; Michael Forte; Silvio Tosatto; Giovanna Lippe; Paolo Bernardi
Journal:  EMBO Rep       Date:  2017-05-15       Impact factor: 8.807

  1 in total

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