30S动力蛋白上的一个高亲和力ATP结合位点。

A high-affinity ATP-binding site on 30S dynein.

作者信息

Blum J J, Hayes A

出版信息

J Supramol Struct. 1979;11(2):117-22. doi: 10.1002/jss.400110202.

PMID:161993

Abstract

The enhancing effect of low concentrations (eg, 8 microM) of bis(4-fluoro-3-nitrophenyl)sulfone (FNS) on 30S dynein ATPase activity is increased when 1 mM dithiothreitol (DTT) is present. The effect of FNS + DTT is optimal at pH 7.5. Activation of the latent ATPase activity of 30S dynein by FNS + DTT is partially prevented by 1--3 microM ATP. Adenylylimidodiphosphate (AMP-PNP) is less effective than ATP, while beta, gamma-methylene-adenosine triphosphase (AMP-PCP), though a much stronger inhibitor of ATPase activity than AMP-PNP, does not protect against enhancement. These results demonstrate the presence of high-affinity ATP-binding site on 30S dynein.

摘要

当存在1 mM二硫苏糖醇（DTT）时，低浓度（如8 microM）的双（4-氟-3-硝基苯基）砜（FNS）对30S动力蛋白ATP酶活性的增强作用会增强。FNS + DTT的作用在pH 7.5时最佳。1-3 microM的ATP可部分阻止FNS + DTT对30S动力蛋白潜在ATP酶活性的激活。腺苷酰亚胺二磷酸（AMP-PNP）的效果不如ATP，而β，γ-亚甲基腺苷三磷酸（AMP-PCP）虽然是比AMP-PNP更强的ATP酶活性抑制剂，但不能防止其增强作用。这些结果证明了30S动力蛋白上存在高亲和力的ATP结合位点。