The external calcium-dependent NADPH dehydrogenase from Neurospora crassa mitochondria

• Type: Article in International Scientific Journal
• Date: 2001

Authors

melo, amp (Author) Other; duarte, m (Author) ICBAS; moller, im (Author) Other; prokisch, h (Author) Other; dolan, pl (Author) Other; pinto, l (Author) Other; nelson, ma (Author) Other; videira, a (Author) ICBAS

Journal

Title: Journal of Biological Chemistry

Vol. 276

Pages: 3947-3951

ISSN: 0021-9258

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 47 Citations

Scopus - 46 Citations

Other information

Authenticus ID: P-000-WDG

DOI: 10.1074/jbc.M008199200

Abstract (EN): We have inactivated the nuclear gene coding for a putative NAD(P)H dehydrogenase from the inner membrane of Neurospora crassa mitochondria by repeat-induced point mutations. The respiratory rates of mito chondria from the resulting mutant (nde-1) were measured, using NADH or NADPH as substrates under different assay conditions. The results showed that the mutant lacks an external calcium-dependent NADPH dehydrogenase. The observation of NADH and NADPH oxidation by intact mitochondria from the nde-1 mutant suggests the existence of a second external NAD(P)H dehydrogenase, The topology of the NDE1 protein was further studied by protease accessibility, in vitro import experiments, and in silico analysis of the amino acid sequence. Taken together, it appears that most of the NDE1 protein extends into the intermembrane space in a tightly folded conformation and that it remains anchored to the inner mitochondrial membrane by an N-terminal transmembrane domain.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5