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Results: 131 to 133 of 133

Publication Record


Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase.
Cook RJ, Lloyd RS, Wagner C
(1991) J Biol Chem 266: 4965-73
MeSH Terms: Amino Acid Sequence, Animals, Bacillus subtilis, Blotting, Southern, Carcinoma, Hepatocellular, DNA, Drosophila melanogaster, Electrophoresis, Agar Gel, Escherichia coli, Humans, Liver, Liver Neoplasms, Molecular Sequence Data, Open Reading Frames, Oxidoreductases Acting on CH-NH Group Donors, Rats, Sequence Alignment, Sequence Homology, Nucleic Acid
Show Abstract · Added January 20, 2015
We have isolated and characterized cDNA clones encoding rat liver cytosol 10-formyltetrahydrofolate dehydrogenase (EC An open reading frame of 2706 base pairs encodes for 902 amino acids of Mr 99,015. The deduced amino acid sequence contains exact matches to the NH2-terminal sequence (28 residues) and the sequences of five peptides derived from cyanogen bromide cleavage of the purified protein. The amino acid sequence of 10-formyltetrahydrofolate dehydrogenase has three putative domains. The NH2-terminal sequence (residues 1-203) is 24-30% identical to phosphoribosylglycinamide formyltransferase (EC from Bacillus subtilis (30%), Escherichia coli (24%), Drosophila melanogaster (24%), and human hepatoma HepG2 (27%). Residues 204-416 show no extensive homology to any known protein sequence. Sequence 417-900 is 46% (mean) identical to the sequences of a series of aldehyde dehydrogenase (NADP+) (EC Intact 10-formyltetrahydrofolate dehydrogenase exhibits NADP-dependent aldehyde dehydrogenase activity. The sequence identity to phosphoribosylglycinamide formyltransferase is discussed, and a binding region for 10-formyltetrahydrofolate is proposed.
0 Communities
1 Members
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18 MeSH Terms
Nucleotide sequence of mouse SCIP cDNA, a POU-domain transcription factor.
Zimmerman EC, Jones CM, Fet V, Hogan BL, Magnuson MA
(1991) Nucleic Acids Res 19: 956
MeSH Terms: Animals, DNA, Mice, Molecular Sequence Data, Octamer Transcription Factor-6, Open Reading Frames, Polymerase Chain Reaction, Rats, Sequence Homology, Nucleic Acid, Transcription Factors
Added May 27, 2010
0 Communities
1 Members
0 Resources
10 MeSH Terms
Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events.
Denison MR, Zoltick PW, Hughes SA, Giangreco B, Olson AL, Perlman S, Leibowitz JL, Weiss SR
(1992) Virology 189: 274-84
MeSH Terms: Leupeptins, Models, Biological, Murine hepatitis virus, Peptide Fragments, Precipitin Tests, Protein Biosynthesis, Protein Precursors, Protein Processing, Post-Translational, Reading Frames, Time Factors, Viral Proteins
Show Abstract · Added February 19, 2015
Several polypeptide products of MHV-A59 ORF 1a were characterized in MHV-A59 infected DBT cells, using antisera directed against fusion proteins encoded in the first 6.5 kb of ORF1a. These included the previously identified N-terminal ORF 1a product, p28, as well as 290-, 240-, and 50-kDa polypeptides. P28 was always detected as a discrete band without larger precursors, suggesting rapid cleavage of p28 immediately after its synthesis. Once p28 was cleaved there was little degradation of the protein over a 2-hr period. The intracellular cleavage of p28 was not inhibited by the protease inhibitor leupeptin, in contrast to results obtained during in vitro translation of genome RNA (Denison and Perlman, 1986). These data suggest that different protease activities may be responsible for the cleavage of p28 in vitro and in vivo. The 290-kDa protein was an intermediate cleavage product derived from a precursor of greater than 400 kDa. The 290-kDa product was subsequently cleaved into secondary products of 50 and 240 kDa. The intracellular cleavage of the 290-kDa polypeptide was inhibited by leupeptin at concentrations which did not inhibit the early cleavage of p28 or the cleavage of the 290-kDa product from its larger polyprotein precursor. In the presence of zinc chloride, a product of greater than 320 kDa was detected, which appears to incorporate p28 at its amino terminus. This suggests that at least two protease activities may be necessary for processing of ORF1a proteins, one of which cleaves p28 and is sensitive to zinc chloride but resistant to leupeptin, and the other which cleaves the 290-kDa precursor and is sensitive to both inhibitors. Both the 290- and 240-kDa proteins should contain sequences predicted to encode two papain-like protease activities.
0 Communities
1 Members
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11 MeSH Terms