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Title: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component of human ketoacid dehydrogenase complexes
Author: Pons i Irazazábal, Gabriel
Raefsky-Estrin, Cindy
Carothers, Donna J.
Pepin, Ronald A.
Javed, Ali A.
Jesse, Barry W.
Ganapathi, Mahrukh K.
Samols, David
Patel, Mulchand S.
Keywords: Seqüència d'aminoàcids
Clonatge molecular
Amino acid sequence
Molecular cloning
Issue Date: 1988
Publisher: National Academy of Sciences
Abstract: cDNA clones comprising the entire coding region for human dihydrolipoamide dehydrogenase (dihydrolipoamide:NAD+ oxidoreductase, EC have been isolated from a human liver cDNA library. The cDNA sequence of the largest clone consisted of 2082 base pairs and contained a 1527-base open reading frame that encodes a precursor dihydrolipoamide dehydrogenase of 509 amino acid residues. The first 35-amino acid residues of the open reading frame probably correspond to a typical mitochondrial import leader sequence. The predicted amino acid sequence of the mature protein, starting at the residue number 36 of the open reading frame, is almost identical (greater than 98% homology) with the known partial amino acid sequence of the pig heart dihydrolipoamide dehydrogenase. The cDNA clone also contains a 3' untranslated region of 505 bases with an unusual polyadenylylation signal (TATAAA) and a short poly(A) track. By blot-hybridization analysis with the cDNA as probe, two mRNAs, 2.2 and 2.4 kilobases in size, have been detected in human tissues and fibroblasts, whereas only one mRNA (2.4 kilobases) was detected in rat tissues.
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It is part of: Proceedings of the National Academy of Sciences of the United States of America - PNAS, 1988, vol. 85, p. 1422-1426
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ISSN: 0027-8424
Appears in Collections:Articles publicats en revistes (Ciències Fisiològiques)

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