Unknown

Dataset Information

0

Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis.


ABSTRACT: We have determined the primary structure of the [2Fe-2S]ferredoxin of the anaerobic protist Trichomonas vaginalis. This protein, situated in the hydrogenosome, is composed of 93 amino acids. A comparison of T. vaginalis ferredoxin with greater than 80 other ferredoxins shows the closest similarity to [2Fe-2S]putidaredoxin of the aerobic bacterium Pseudomonas putida and a lesser one to mitochondrial [2Fe-2S]ferredoxins of vertebrates. This similarity is reflected in the overall primary structure and in the spacing of cysteine residues coordinating the iron-sulfur center. The primary structure, but not the environment of the iron-sulfur center, also shows similarity with [2Fe-2S]ferredoxins of photosynthetic organisms and halobacteria. We have cloned and analyzed the T. vaginalis ferredoxin gene. The gene is present in a single copy and devoid of introns. It gives rise to a transcript with unusually short 5' and 3' untranslated regions of 16 and 18 nucleotides, respectively. DNA sequence analysis of the gene predicts an additional 8 amino acids at the amino terminus which are absent from the purified protein. This amino-terminal region of the protein is characterized by properties typical of mitochondrial presequences.

SUBMITTER: Johnson PJ 

PROVIDER: S-EPMC54479 | biostudies-other | 1990 Aug

REPOSITORIES: biostudies-other

altmetric image

Publications

Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis.

Johnson P J PJ   d'Oliveira C E CE   Gorrell T E TE   Müller M M  

Proceedings of the National Academy of Sciences of the United States of America 19900801 16


We have determined the primary structure of the [2Fe-2S]ferredoxin of the anaerobic protist Trichomonas vaginalis. This protein, situated in the hydrogenosome, is composed of 93 amino acids. A comparison of T. vaginalis ferredoxin with greater than 80 other ferredoxins shows the closest similarity to [2Fe-2S]putidaredoxin of the aerobic bacterium Pseudomonas putida and a lesser one to mitochondrial [2Fe-2S]ferredoxins of vertebrates. This similarity is reflected in the overall primary structure  ...[more]

Similar Datasets

| S-EPMC1148305 | biostudies-other
| S-EPMC1853131 | biostudies-literature
| S-EPMC3887241 | biostudies-literature
| S-EPMC1406841 | biostudies-literature
| S-EPMC26183 | biostudies-literature
| S-EPMC2725143 | biostudies-literature
| S-EPMC7844918 | biostudies-literature
| S-EPMC5663105 | biostudies-literature
| S-EPMC4021607 | biostudies-literature
| S-EPMC7845603 | biostudies-literature