Nucleotide bindind by the synapse associated protein SAP90

FEBS Letters

Linial, Michal²  Kistner, Ute²  Garner, Craig C.¹ 

[1] UAB-Neurobiology Res. Center, 1719 Sixth Ave. S., Birmingham, AL 35213-0021, USA;Department of Biological Chemistry, Institute of Life Sciences, The Hebrew University, Jerusalem 91904, Israel

关键词: Dlg-A;    Guanylate kinase;    Nucleotide binding;    Synaptic protein;    aa;    amino acid;    ABTS;    2;    2′-Azinobis (3-ethylbenzthiazoline) sulfonic Acid;    ELISA;    enzyme-linked immunosorbent assay;    GK;    guanylate kinase;    GST;    glutathione-S-transferase;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(95)00030-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The rat synapse associated protein SAP90 is a member of a superfamily of potential guanylate kinases localized at cell-cell contact sites. This superfamily includes the synapse associated protein SAP97, a close relative of SAP90, the Drosophila tumor suppressor gene product dlg-Ap, the mammalian zonula occludens proteins ZO-1 and ZO-2 and the erythrocyte protein p55. Here we show that SAP90 specifically binds GMP in the micromolar range while binding to ATP, GDP and ADP is at a much lower affinity (10–25 mM), whether or not binding is detected for other guanine and adenine nucleotides. No guanylate kinase activity of SAP90 was detected under our experimental conditions. The importance of the GMP binding capacity per se and an evolutionary role for conserving of the guanylate kinase domain in this superfamily are discussed.

【 授权许可】

Unknown