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Literature summary for 1.3.5.1 extracted from

  • Gawryluk, R.M.; Gray, M.W.
    A split and rearranged nuclear gene encoding the iron-sulfur subunit of mitochondrial succinate dehydrogenase in Euglenozoa (2009), BMC Res. Notes, 2, 16.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.5.1

Application

Application Comment Organism
molecular biology the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria. The discovery of this unique molecular marker provides evidence for the monophyly of Euglenozoa that is independent of evolutionary models Euglena gracilis
molecular biology the splitting of sdhB in Euglena and trypanosomatids is an example of a unique molecular character that specifically unites these two phylogenetic groups Euglena gracilis
molecular biology the splitting of sdhB in Euglena and trypanosomatids is an example of a unique molecular character that specifically unites these two phylogenetic groups Trypanosoma brucei
molecular biology the splitting of sdhB in Euglena and trypanosomatids is an example of a unique molecular character that specifically unites these two phylogenetic groups Reclinomonas americana

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Euglena gracilis 5739
-
mitochondrion
-
 Trypanosoma brucei 5739
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mitochondrion
-
 Reclinomonas americana 5739
-
mitochondrion based on the presence of a predicted mitochondrial targeting peptides the protein is imported into mitochondria Euglena gracilis 5739
-

Organism

Organism UniProt Comment Textmining
Euglena gracilis
-
-
-
Reclinomonas americana
-
-
-
Trypanosoma brucei
-
-
-

Synonyms

Synonyms Comment Organism
SDHB iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase Euglena gracilis
SDHB iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase Trypanosoma brucei
SDHB iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase Reclinomonas americana

General Information

General Information Comment Organism
physiological function the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional Euglena gracilis
physiological function the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional Trypanosoma brucei
physiological function the iron-sulfur subunit (SdhB) of mitochondrial succinate dehydrogenase is encoded by a split and rearranged nuclear gene in Euglena gracilis and trypanosomatids, an example of a rare genomic character. The two subgenic modules are transcribed independently and the resulting mRNAs appear to be independently translated, with the two protein products imported into mitochondria, based on the presence of predicted mitochondrial targeting peptides. Although the inferred protein sequences are in general very divergent from those of other organisms, all of the required iron-sulfur cluster-coordinating residues are present. Moreover, the discontinuity in the euglenozoan SdhB sequence occurs between the two domains of a typical, covalently continuous SdhB, consistent with the inference that the euglenozoan half proteins are functional Reclinomonas americana