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Cloning and sequence analysis of a cDNA encoding rice glutaredoxin
Author(s) -
Minakuchi Kazunobu,
Yabushita Tetsushige,
Masumura Takehiro,
Ichihara Ken'ichi,
Tanaka Kunisuke
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80264-5
Subject(s) - complementary dna , peptide sequence , biology , sequence analysis , glutaredoxin , cloning (programming) , cdna library , amino acid , microbiology and biotechnology , polyadenylation , genetics , gene , messenger rna , computer science , thioredoxin , programming language
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.