https://scholars.lib.ntu.edu.tw/handle/123456789/160022
標題: | Molecular Characterization of a Conserved, Guanine Nucleotide-Dependent Adp-Ribosylation Factor in Drosophila Melanogaster | 作者: | JAMES J. MURTAGH LEE, FANG-JEN S PETER DEAK LINDA M. HALL LUCIA MONACO LEE, CHII-MING LINDA A. STEVENS JOEL MOSS MARTHA VAUGHAN |
關鍵字: | GTP-BINDING PROTEINS;GLUTATHIONE-S-TRANSFERASE;POLYMERASE CHAIN-REACTION;CHOLERA-TOXIN;ADENYLATE-CYCLASE | 公開日期: | 1993 | 卷: | v.32 | 期: | n.23 | 起(迄)頁: | 6011-6018 | 來源出版物: | BIOCHEMISTRY | 摘要: | ADP-Ribosylation factors (ARFs) are ubiquitous approximately 20-kDa guanine nucleotide-binding proteins that stimulate cholera toxin-catalyzed ADP-ribosylation in vitro. Because the functional role(s) of ARF in mammalian systems is (are) elusive, we looked for ARF in Drosophila melanogaster, and report the partial purification and molecular cloning of an ARF from Drosophila. We cloned the Drosophila ARF 1 gene without library screening by a combination of 5 polymerase chain reactions (PCRs), yielding a 546-base open reading frame encoding 182 amino acids, which are> 93% identical to those of mammalian class I ARFs. This ARF gene maps to 79F3- 6 in the proximal region of the left arm of Drosophila chromosome 3. The Drosophila ARF1 gene structure, including placement of introns, is highly conserved relative to mammalian class 1 ARF genes. A single ARF mRNA species of 1. 8 kb was abundant in all Drosophila body segments. Recombinant Drosophila ARF 1 synthesized in Escherichia coli had biochemical and immunochemical activities similar to those of mammalian ARF. The similarities of sequence and biochemical properties between Drosophila and mammalian ARFs contrast with their differences from Drosophila arl (ARF- like protein), which does not stimulate cholera toxin - catalyzed ADP-ribosylation, and is only approximately 52-56% identical in amino acid sequence to mammalian ARFs. |
URI: | http://ntur.lib.ntu.edu.tw//handle/246246/92448 |
顯示於: | 分子醫學研究所 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。