The N-terminal region is important for the nuclease activity and thermostahility of the flap endonuclease-1 from Sulfolobus tokodaii

被引：6

作者：

Horie, Masanori

Fukui, Koichi

Xie, Minjue

Kageyama, Yoshitaka

Hamada, Kazuo

Sakihama, Yuri

Sugimori, Kenji

Matsumoto, Kazuko

机构：

[1] Japan Sci & Technol Agcy, Preventure Program, Off Technol Transfer, Chiyoda Ku, Tokyo 1028666, Japan

[2] Toho Univ, Sch Med, Dept Biol, Ota Ku, Tokyo 1438540, Japan

[3] Waseda Univ, Dept Chem, Adv Res Ctr Sci & Engn, Shinjuku Ku, Tokyo 1698555, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2007年 / 71卷 / 04期

关键词：

flap endonuclease; Sulfolobus tokodaii; Thermoplasma acidophilum;

D O I：

10.1271/bbb.60326

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This paper reports the biochemical properties of two types of recombinant flap endonuclease-1 (FEN-1) proteins obtained from the thermophilic crenarchaeon, Sulfolobus tokodaii strain 7. One of the two FEN-1 proteins is a product of the gene with AUG as the translational start codon (StoS-FEN-1), which is originally assigned in the database. The other is a product of the gene with a new AUG start codon (StoL-FEN-1), which is inserted at 153 bases upstream of the original AUG codon. Although StoL-FEN-1 showed activity and thermostability, StoS-FEN-1 showed neither activity nor thermostability. The N-terminal region in StoL-FEN-1 was also conserved in all of the FEN-1 homologs deduced from genes from newly isolated Sulfolobus spp. These results strongly suggest that the actual start codon of the fen-1 gene from S. tokodaii is not the originally assigned AUG, but rather is located at about 100 bases upstream of this codon.

引用

页码：855 / 865

页数：11