ArticleMolecular biology of the cell2001
MAP-1 and IAP-1, two novel AAA proteases with catalytic sites on opposite membrane surfaces in mitochondrial inner membrane of Neurospora crassa.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Anilinopyrimidine Resistance inFrontiers in microbiology · 2017Article
- YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress.EMBO reports · 2015Article
- A second eukaryotic group with mitochondrion-encoded tmRNA: in silico identification and experimental confirmation.RNA biology · 2013Article
- Unmasking a temperature-dependent effect of the P. anserina i-AAA protease on aging and development.Cell cycle (Georgetown, Tex.) · 2011Article
- Supramolecular organization of the respiratory chain in Neurospora crassa mitochondria.Eukaryotic cell · 2007Article
- Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion.The Journal of cell biology · 2007Article
- Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane space.Molecular and cellular biology · 2007Article
- Plant mitochondria contain at least two i-AAA-like complexes.Plant molecular biology · 2005Article
- Mutation detection in four candidate genes (OXA1L, MRS2L, YME1L and MIPEP) for combined deficiencies in the oxidative phosphorylation system.Journal of inherited metabolic disease · 2005Article
- Science in motion: common molecular pathological themes emerge in the hereditary spastic paraplegias.Journal of medical genetics · 2003Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic AAA proteases form a conserved family of membrane-embedded ATP-dependent proteases but have been analyzed functionally only in the yeast Saccharomyces cerevisiae. Here, we have identified two novel members of this protein family in the filamentous fungus Neurospora crassa, which were termed MAP-1 and IAP-1. Both proteins are localized to the inner membrane of mitochondria. They are part of two similar-sized high molecular mass complexes, but expose their catalytic sites to opposite membrane surfaces, namely, the intermembrane and the matrix space. Disruption of iap-1 by repeat-induced point mutation caused a slow growth phenotype at high temperature and stabilization of a misfolded inner membrane protein against degradation. IAP-1 could partially substitute for functions of its yeast homolog Yme1, demonstrating functional conservation. However, respiratory growth at 37 degrees C was not restored. Our results identify two components of the quality control system of the mitochondrial inner membrane in N. crassa and suggest that AAA proteases with catalytic sites exposed to opposite membrane surfaces are present in mitochondria of all eukaryotic cells.
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