Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion.
Traffic
; 8(5): 500-11, 2007 May.
Article
em En
| MEDLINE
| ID: mdl-17451553
ABSTRACT
The outer mitochondrial membrane protein Ugo1 forms a complex with the Fzo1p and Mgm1p GTPases that regulates mitochondrial fusion in yeast. Ugo1p contains two putative carrier domains (PCDs) found in mitochondrial carrier proteins (MCPs). Mitochondrial carrier proteins are multipass transmembrane proteins that actively transport molecules across the inner mitochondrial membrane. Mitochondrial carrier protein transport requires functional carrier domains with the consensus sequence PX(D/E)XX(K/R). Mutation of charged residues in this consensus sequence disrupts transport function. In this study, we used targeted mutagenesis to show that charge reversal mutations in Ugo1p PCD2, but not PCD1, disrupt mitochondrial fusion. Ugo1p is reported to be a single-pass transmembrane protein despite the fact that it contains several additional predicted transmembrane segments. Using a combination of protein targeting and membrane extraction experiments, we provide evidence that Ugo1p contains additional transmembrane domains and is likely a multipass transmembrane protein. These studies identify PCD2 as a functional domain of Ugo1p and provide the first experimental evidence for a multipass topology of this essential fusion component.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Saccharomyces cerevisiae
/
Proteínas de Fusão de Membrana
/
Fusão de Membrana
/
Proteínas de Membrana
/
Mitocôndrias
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Traffic
Assunto da revista:
FISIOLOGIA
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Estados Unidos