These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Molecular characterization of the alpha-subunit of Trichomonas vaginalis hydrogenosomal succinyl CoA synthetase.
    Author: Lahti CJ, Bradley PJ, Johnson PJ.
    Journal: Mol Biochem Parasitol; 1994 Aug; 66(2):309-18. PubMed ID: 7808480.
    Abstract:
    The anaerobic, parasitic protist, Trichomonas vaginalis, is characterized by the absence of mitochondria and the presence of double membrane bound organelles called hydrogenosomes. Succinyl-coenzyme A synthetase is a hydrogenosomal enzyme which catalyzes the formation of ATP via substrate-level phosphorylation. We have characterized genes encoding the alpha subunit of the hydrogenosomal protein succinyl-coenzyme A synthetase (SCS). The alpha-SCS of T. vaginalis is encoded by a multigene family composed of 3 similar genes that do not appear allelic. These 3 alpha-SCS genes encode a protein with a calculated molecular mass of approximately 32.5 kDa that has > 50% identity (> 70% similarity with alpha-SCSs from Escherichia coli, Thermus flavus, and rat liver mitochondria. Antibodies raised against recombinant T vaginalis alpha-SCS expressed in bacteria were used to isolate alpha-SCS proteins from purified hydrogenosomes. These proteins partition into the soluble fraction of hydrogenosomes treated with sodium carbonate at high pH, consistent with a matrix localization in the organelle. Amino-terminal sequencing of purified alpha-SCS proteins shows that mature proteins lack a short, leader sequence of 9 amino acids. These amino terminal sequences which are cleaved from T. vaginalis alpha-SCSs are similar to each other and to all other leader sequences identifed on hydrogenosomal proteins.
    [Abstract] [Full Text] [Related] [New Search]