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

• Type: Article in International Scientific Journal
• Date: 2013

Authors

Pereira, B (Author) Other; Videira, A (Author) ICBAS; Duarte, M (Author) Other

Journal

Title: Molecular and Cellular Biology

Vol. 33

Pages: 2623-2634

ISSN: 0270-7306

Publisher: American Society for Microbiology

Indexing

ISI Web of Knowledge - 0 Citations

Scopus - 0 Citations

Scientific classification

FOS: Natural sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific