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PubMed · 8287970

Cloning and sequence analysis of a cDNA encoding rice glutaredoxin.

K Minakuchi·T Yabushita·T Masumura·K Ichihara·K Tanaka
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Abstract

A full-length cDNA clone (RASC8) encoding glutaredoxin (thioltransferase) was isolated from a cDNA library of an aleurone layer prepared from a developing seed of rice (Oryza sativa L.). RASC8, 568bp in length, contained an ATG codon and two possible polyadenylation signals, and encoded 112 amino acid residues. Cys-Pro-Phe-Cys, which is the active site and a highly conserved sequence among thioltransferases, was found in the deduced amino acid sequence. RASC8 was introduced into an expression vector pMALc2 and the translated product possessed thioltransferase activity.

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Amino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA, ComplementaryGene LibraryGenes, PlantGlutaredoxinsMolecular Sequence DataOryzaOxidoreductasesPlant ProteinsProtein BiosynthesisProtein Disulfide Reductase (Glutathione)ProteinsRecombinant Fusion ProteinsSequence Homology, Amino AcidSwineComparative StudyJournal Article

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K Minakuchi, T Yabushita, T Masumura, K Ichihara, K Tanaka. 1994-01-10. Cloning and sequence analysis of a cDNA encoding rice glutaredoxin.. https://doi.org/10.1016/0014-5793(94)80264-5

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