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Nucleotide-dependent bisANS binding to tubulin.

S Chakraborty1, N Sarkar, B Bhattacharyya

  • 1Department of Biochemistry, Bose Institute, Centenary Building, P-1/12 C.I.T. Scheme VII M, Calcutta 700054, India.

Biochimica Et Biophysica Acta
|July 17, 1999
PubMed
Summary
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The hydrophobic probe bisANS binds specifically to tubulin at one high-affinity site with guanosine 5'-triphosphate (GTP). Without GTP, bisANS binding is non-specific, altering tubulin structure and activity.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Non-covalent hydrophobic probes like bisANS are used to study protein structure.
  • Non-specific binding of bisANS to multiple protein sites limits its utility.
  • Specific binding conditions are crucial for accurate dye-protein interaction studies.

Purpose of the Study:

  • To investigate the specific binding of bisANS to tubulin.
  • To determine the influence of guanosine 5 -triphosphate (GTP) on bisANS-tubulin interaction.
  • To understand the structural consequences of bisANS binding to tubulin.

Main Methods:

  • Spectroscopic analysis of bisANS binding to tubulin.
  • Assessing tubulin secondary structure changes.
  • Monitoring colchicine binding activity of tubulin.

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Main Results:

  • BisANS binds instantaneously and specifically to a high-affinity site on tubulin in the presence of 1 mM GTP.
  • In the absence of GTP, bisANS binding is non-specific, time-dependent, and leads to loss of tubulin secondary structure and colchicine binding activity.
  • GTP and other nucleotide analogs (GDP, GMP, ATP) displace bisANS from lower-affinity sites.

Conclusions:

  • GTP facilitates specific, high-affinity bisANS binding to tubulin.
  • Nucleotide-induced structural changes in tubulin may generate multiple low-affinity binding sites for bisANS.
  • GTP and other nucleotides protect tubulin from bisANS-induced structural alterations.