PMID: 8595866Jan 15, 1996Paper

Primary structure of a cytosolic malate dehydrogenase of the amitochondriate eukaryote, Trichomonas vaginalis

FEMS Microbiology Letters
A MarkosM Müller

Abstract

The nucleotide sequence of a gene coding for a 37 kDa subunit of a cytosolic malate dehydrogenase of Trichomonas vaginalis was established. The sequence of a gDNA clone and a cDNA clone, which lacked seven amino-terminal codons, were identical, indicating an absence of introns from the gene. Cell fractionation combined with sequencing of peptide fragments of the purified enzyme showed that the gene codes for an expressed cytosolic enzyme. The derived amino acid sequence was closely related to cytosolic malate dehydrogenases from animals and plants and from the eubacteria Thermus aquaticus and Mycobacterium leprae and was more distant from the enzyme of mitochondria and from Escherichia coli and certain other eubacteria. In phylogenetic reconstructions this enzyme shared a most recent common ancestor with other cytosolic enzymes.

References

Dec 1, 1991·Current Opinion in Genetics & Development·M L Sogin
Jan 1, 1988·Annual Review of Microbiology·M Müller
May 1, 1988·Trends in Biochemical Sciences·L McAlister-Henn
Oct 1, 1988·Sexually Transmitted Diseases·E M ProctorW R Bowie
Dec 1, 1974·Experimental Parasitology·H Dowda, H O Betterton

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Citations

May 26, 1999·Proceedings of the National Academy of Sciences of the United States of America·G WuM Müller
Dec 5, 2008·FEMS Microbiology Letters·Alexander S ReshetnikovYuri A Trotsenko
Oct 17, 2006·Parasitology Today·D R Liston, P J Johnson

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