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Lookup NU author(s): Professor Robert HirtORCiD, Emeritus Professor T. Martin Embley FMedSci FRSORCiD
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The hydrogenosomal malic enzyme (ME) was purified from the anaerobic fungus Neocallimastix frontalis. Using reverse genetics, the corresponding cDNA was isolated and characterized. The deduced amino acid sequence of the ME showed high similarity to ME from metazoa, plants and protists. Putative functional domains for malate and NAD+/NADP+ binding were identified. Phylogenetic analysis of the deduced amino acid sequence of the new ME suggests that it is homologous to reference bacterial and eukaryotic ME. Most interestingly, the cDNA codes for a protein which contains a 27-amino-acid N-terminus which is not present on the purified mature protein. This presequence shares features with known mitochondrial targeting signals, including an enrichment in Ala, Leu, Ser, and Arg, and the presence of an Arg at position-2 relative to amino acid 1 of the mature protein. This is the first report of a mitochondrial-like targeting signal on a hydrogenosomal enzyme from an anaerobic fungus and provides support for the hypothesis that hydrogenosomes in Neocallimastix frontalis might be modified mitochondria.
Author(s): Embley TM; Hirt RP; van der Giezen M; Rechinger KB; Svendsen I; Durand R; Fevre M; Prins RA
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Year: 1997
Volume: 23
Issue: 1
Pages: 11-21
Print publication date: 01/01/1997
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: Wiley-Blackwell
URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9004216
