Identification of a Novel selD Homolog from Eukaryotes, Bacteria, and Archaea: Is there an Autoregulatory Mechanism in Selenocysteine Metabolism?

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 93; no. 26; pp. 15086 - 15091
• Main Authors: Guimaraes, M. Jorge, Peterson, David, Vicari, Alain, Cocks, Benjamin G., Copeland, Neal G., Gilbert, Debra J., Jenkins, Nancy A., Ferrick, David A., Kastelein, Robert A., Bazan, J. Fernando, Zlotnik, Albert
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 24.12.1996; National Acad Sciences; National Academy of Sciences; The National Academy of Sciences of the USA
• Subjects: Amino Acid Sequence; Animals; Archaea - genetics; Archaea - metabolism; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Base Sequence; Biochemistry; Biological Sciences; Chromosome Mapping; Chromosomes; Cloning, Molecular; Codons; Complementary DNA; COS Cells; Drosophila Proteins; Enzymes; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Female; Genes; Genetic loci; Genetic Markers; Haemophilus influenzae; Humans; Metabolism; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Molecules; Phosphotransferases; Phylogeny; Polymerase Chain Reaction; Proteins; Selenium - metabolism; Selenocysteine - metabolism; Selenoproteins; Sequence Homology, Amino Acid; T lymphocytes; Transfection; Untranslated regions

Escherichia coli selenophosphate synthetase (SPS, the selD gene product) catalyzes the production of monoselenophosphate, the selenium donor compound required for synthesis of selenocysteine (Sec) and seleno-tRNAs. We report the molecular cloning of human and mouse homologs of the selD gene, designa...