ArticleJournal of bacteriology1992
Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences.
Article in Journal of bacteriology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 70 citations in OpenAlex.
- The diversity of terminal electron acceptors across eukaryotes.Trends in biochemical sciences · 2026Review
- Extreme mitochondrial reduction in a novel group of free-living metamonads.Nature communications · 2024Article
- An in vitro characterisation of the Trichomonas vaginalis TATA box-binding proteins (TBPs).Parasitology research · 2019Article
- Biochemistry and evolution of anaerobic energy metabolism in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2012Review
- The Trichomonas vaginalis hydrogenosome proteome is highly reduced relative to mitochondria, yet complex compared with mitosomes.International journal for parasitology · 2011Article
- Localization and nucleotide specificity of Blastocystis succinyl-CoA synthetase.Molecular microbiology · 2008Article
- Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis.Molecular microbiology · 2003Article
- Presence of a member of the mitochondrial carrier family in hydrogenosomes: conservation of membrane-targeting pathways between hydrogenosomes and mitochondria.Molecular and cellular biology · 2000Article
- Inhibition of polyamine synthesis arrests trichomonad growth and induces destruction of hydrogenosomes.Antimicrobial agents and chemotherapy · 1999Article
- Clinical and microbiological aspects of Trichomonas vaginalis.Clinical microbiology reviews · 1998Review
- A common evolutionary origin for mitochondria and hydrogenosomes.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis.Journal of molecular evolution · 1995Article
- Similarity between a ubiquitous promoter element in an ancient eukaryote and mammalian initiator elements.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Cloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase.Protein science : a publication of the Protein Society · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We describe studies directed toward understanding the biogenesis and origin of the hydrogenosome, an unusual organelle found exclusively in certain anaerobic eukaryotes that lack mitochondria. Hydrogenosomes are involved in fermentative carbohydrate metabolism and are proposed to have arisen through conversion of mitochondria or via endosymbiosis with an anaerobic bacterium. We cloned a gene encoding the beta subunit of the hydrogenosomal protein succinyl-coenzyme A synthetase (beta-SCS) and isolated the protein from Trichomonas vaginalis. The T. vaginalis beta-SCS gene encodes a protein with a calculated molecular mass of 43,980 Da that has 43% amino acid identity (65% similarity) with beta-SCS from Escherichia coli. The trichomonad protein partitions into the soluble fraction of hydrogenosomes treated with sodium carbonate at high pH, consistent with a matrix localization within the organelle. The protein is encoded by a multigene family composed of at least three members. Amino-terminal sequencing of beta-SCS purified from T. vaginalis hydrogenosomes shows that the mature protein lacks the first nine amino acids encoded in the gene. This apparent amino-terminal leader sequence is strikingly similar to that of another hydrogenosomal protein and to mitochondrial presequences.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.