Novel Insights into the Role of Neurospora crassa NDUFAF2, an Evolutionarily Conserved Mitochondrial Complex I Assembly Factor

• Tipo: Artigo em Revista Científica Internacional
• Data: 2013

Autores

Pereira, B (Autor) Outra; Videira, A (Autor) ICBAS; Duarte, M (Autor) Outra

Revista

Título: Molecular and Cellular Biology

Vol. 33

Páginas: 2623-2634

ISSN: 0270-7306

Editora: American Society for Microbiology

Indexação

ISI Web of Knowledge - 0 Citações

Scopus - 0 Citações

Classificação Científica

FOS: Ciências exactas e naturais

Outras Informações

ID Authenticus: P-004-ZV2

DOI: 10.1128/MCB.01476-12

Abstract (EN): Complex I deficiency is commonly associated with mitochondrial oxidative phosphorylation diseases. Mutations in nuclear genes encoding structural subunits or assembly factors of complex I have been increasingly identified as the cause of the diseases. One such factor, NDUFAF2, is a paralog of the NDUFA12 structural subunit of the enzyme, but the mechanism by which it exerts its function remains unknown. Herein, we demonstrate that the Neurospora crassa NDUFAF2 homologue, the 13.4L protein, is a late assembly factor that associates with complex I assembly intermediates containing the membrane arm and the connecting part but lacking the N module of the enzyme. Furthermore, we provide evidence that dissociation of the assembly factor is dependent on the incorporation of the putative regulatory module composed of the subunits of 13.4 (NDUFA12), 18.4 (NDUFS6), and 21 (NDUFS4) kDa. Our results demonstrate that the 13.4L protein is a complex I assembly factor functionally conserved from fungi to mammals.

Idioma: Inglês

Tipo (Avaliação Docente): Científica