biostudies-literatureKraus JPNIADDK NIH HHSNIGMS NIH HHS8049-53https://www.ebi.ac.uk/biostudies/studies/S-EPMC386864biostudies-literatureUnknown83(21)A cDNA encoding the cytoplasmic precursor of the beta subunit of the mitochondrial enzyme propionyl-CoA carboxylase (EC 6.4.1.3) was cloned and sequenced. The DNA sequence of 2070 nucleotides is almost identical in size to the major hybridizing mRNA from rat liver (2000 +/- 50 nucleotides), suggesting that the cloned DNA represents nearly all of the mRNA sequence. A polypeptide expressed in vitro from an mRNA transcript of this cDNA is indistinguishable in size from the beta subunit precursor (58,500 Da). An open reading frame of 1623 nucleotides, flanked by stop codons, encodes a polypeptide of 541 amino acids; the predicted amino acid sequence was confirmed as that of the beta subunit of propionyl-CoA carboxylase by matching it to the amino acid sequences of five peptides derived from puProceedings of the National Academy of Sciences of the United States of AmericaCoding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.PMC386864GM31359AM09527AM12579Rosenberg LEKraus JPFirgaira FNovotny JWilliamson COhura TWilliams KRKalousek FfalseCoding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.A cDNA encoding the cytoplasmic precursor of the beta subunit of the mitochondrial enzyme propionyl-CoA carboxylase (EC 6.4.1.3) was cloned and sequenced. The DNA sequence of 2070 nucleotides is almost identical in size to the major hybridizing mRNA from rat liver (2000 +/- 50 nucleotides), suggesting that the cloned DNA represents nearly all of the mRNA sequence. A polypeptide expressed in vitro from an mRNA transcript of this cDNA is indistinguishable in size from the beta subunit precursor (58,500 Da). An open reading frame of 1623 nucleotides, flanked by stop codons, encodes a polypeptide of 541 amino acids; the predicted amino acid sequence was confirmed as that of the beta subunit of propionyl-CoA carboxylase by matching it to the amino acid sequences of five peptides derived from pu1986-01-01T00:00:00Z1986 Nov2025-04-18T16:45:28.625Z2025-04-07T04:08:25.55ZS-EPMC386864346494210.1073/pnas.83.21.8049