Calcium‐dependent interaction of annexin I with annexin II and mapping of the interaction sites

FEBS Letters

Kim, Jung Woo²  Na, Doe Sun¹  Lee, Kyoung Hoa² 

[1] Department of Biochemistry, College of Medicine, University of Ulsan, Seoul 138-040, South Korea;Division of Life Science, Pai Chai University, 439-6 Doma-dong, Seo-gu, Taejon 302-735, South Korea

关键词: Annexin I;    Annexin II;    Ca2+ dependence;    Specific binding;    Two-hybrid assay;    ANX1;    annexin I;    ANX2;    annexin II;    X-gal;    5-bromo-4-chloro-3-indolyl-d-galactopyranoside;    ONPG;    o-nitrophenyl β-d-galactopyranoside;    MBP;    maltose-binding protein;   

DOI  :  10.1016/S0014-5793(98)01643-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Annexins are multifunctional intracellular proteins with Ca²⁺- and phospholipid-binding properties. Their structures consist of four conserved repeat domains that form the core and a diverse N-terminal tail, from which their functional differences may arise. We searched for cellular proteins that interact with the N-terminal tail plus domain I of annexin I (ANX1) by using the yeast two-hybrid method. Screening of a HeLa cell cDNA library yielded annexin II (ANX2) cDNA. The interaction between ANX1 and ANX2 also occurred in vitro in a Ca²⁺-dependent manner. Mapping of the interaction sites revealed that interaction between domain I of ANX1 and domain IV of ANX2 was stronger than the other combinations.

【 授权许可】

Unknown