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

✍ Scribed by Blum, J. J. ;Hayes, A.

• Book ID: 102440218
• Publisher: Wiley (John Wiley & Sons)
• Year: 1979
• Tongue: English
• Weight: 330 KB
• Volume: 11
• Category: Article
• ISSN: 0091-7419
• DOI: 10.1002/jss.400110202

✦ Synopsis

The enhancing effect of low concentrations (eg, 8 pM) of bis(4-fluoro-3-nitropheny1)sulfone (FNS) on 3 0 s 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 pM ATP. Adenylylimidodiphosphate (AMP-PNP) is less effective than ATP, while P,y-methylene-adenosine triphosphate (AMP-PCP), though a much stronger inhibitor of ATPase activity than AMP-PNP, does not protect against enhancement. These results demonstrate the presence of a high-affinity ATP-binding site on 30s dynein.