caa a22 4500 397558562 CHVBK 20180308164810.0 cr unu---uuuuu 161202e199611 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021497 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021497 Isolation and Characterization of ECTl Gene Encoding CTP: Phosphoethanolamine Cytidylyltransferase of Saccharomyces cerevisiae [Elektronische Daten] [Rho Min-Seek, Yuji Kawamata, Hidemitsu Nakamura, Akinori Ohta, Masamichi Takagi] Sacchammyces cerevisiae mutants that were unable to utilize extracellular ethanolamine for phosphatidylethanolamine synthesis were isolated. Two of them carried recessive chromosomal mutations in a same gene and were defective in CTP:phosphoethanolamine cytidylyltransferase (ECT) activity in vitro (Ect−). In an Ect− mutant that also carried the chol mutation, phosphatidylethanolamine accounted for less than 2% of total phospholipids, suggesting the importance of ECT in phosphatidylethanolamine synthesis. By screening a genomic library on a low copy number vector, three complementary clones of different size were isolated. A 2.8-kb common DNA region carried an open reading frame (ORF) of 969 bp in length, of which a truncated form failed to complement the Ect− mutation. This ORF was identical to the previously isolated MUQ1 gene of unknown function. Its deduced amino acid sequence had significant similarity to CTP:phosphocholine cytidylyltransferases of yeast and rat. The entire ORF, when combined with the glutathione Stransferase gene and expressed in Escherichia coli, exhibited ECT activity. These results indicate that the cloned gene encodes a catalytic subunit of ECT of S. cereuisiae. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence CDP-ethanolamine nationallicence Kennedy pathway nationallicence phosphatidylethanolamine nationallicence phosphoethanolamine cytidylyltransferase nationallicence Saccharomyces cerevisiae nationallicence Min-Seek Rho Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut Kawamata Yuji Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut Nakamura Hidemitsu Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut Ohta Akinori Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut Takagi Masamichi Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 120/5(1996-11), 1040-1047 0021-924X 120:5<1040 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021497 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021497 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Min-Seek Rho Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Kawamata Yuji Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Nakamura Hidemitsu Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Ohta Akinori Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Takagi Masamichi Department of Biochemistry The University of Tojyo University, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/5(1996-11), 1040-1047 0021-924X 120:5<1040 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford