caa a22 4500 397555520 CHVBK 20180308164800.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021539 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021539 Isolation and Expression of a Xenopus laevis DNA Methyltransferase cDNA [Elektronische Daten] [Hironobu Kimura, Goshi Ishihara, Shoji Tajima] A Xenopus DNA methyltransferase cDNA was isolated from a Xenopus oocyte cDNA library by screening with the mouse DNA methyltransferase cDNA as a probe. The elucidated nucleotide sequence gave a 4,470 nucleotide open reading frame, and the predicted protein was composed of 1,490 amino acid residues, showing high homology to animal DNA methyltransferases, especially in the catalytic domain in the carboxyl terminal region. The cysteine-rich region and the Lys-Gly repeat which were first found in the mouse sequence were conserved in Xenopus. However, 200 amino acid residues at the amino-terminus of Xenopus DNA methyl transferase were quite different from those of mouse and human, but showed 70% homology with those of chicken. The cloned Xenopus DNA methyltransferase cDNA expressed in COS1 cells showed a significant DNA methyltransferase activity. The size of the translation product of Xenopus DNA methyltransferase cDNA expressed in COS1 cells was identical with that of the endogenous DNA methyltransferase in Xenopus A6 cells and also with the size of newly synthesized DNA methyltransferase in Xenopus oocytes. However, a slightly larger immunoreactlve band of about 205 kDa, and a small iminunoreactive band of about 100 kDa, which were poorly labeled by short incubation with radiolabeled amino acids, were the main bands in stage I-III and stage IV-VI oocytes, respectively. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence cDNA cloning nationallicence DNA methyltransferase nationallicence Xenopus laevis nationallicence Kimura Hironobu Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565 aut Ishihara Goshi Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565 aut Tajima Shoji Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1182-1189 0021-924X 120:6<1182 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021539 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021539 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kimura Hironobu Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Ishihara Goshi Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Tajima Shoji Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1182-1189 0021-924X 120:6<1182 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