Characterization of Capsicum annuum recombinant alpha- and beta-tubulin

Appl Biochem Biotechnol. 2010 Jan;160(1):122-8. doi: 10.1007/s12010-008-8489-4. Epub 2009 Jan 6.

Abstract

There are several conditions which might modulate polymerization to produce polymers having normal lattice structure. In the absence of 1 mM MgCl(2) the assembly was reduced by 36% in Capsicum annuum tubulin (CAnm tubulin). There was no significant difference in the final assembly formation in the presence of 5% to 10% glycerol. However, nucleation rate was slow and apparent study state was achieved lately in the presence of 10% glycerol. Taxol at 100 microM concentration increased 23% tubulin assembly. One millimolar CaCl(2), >or=1% dimethyl sulfoxide (DMSO) and physiologically low temperature reduced CAnm tubulin assembly. A value of 0.089 mg/ml was obtained as critical concentration for polymerization. Benomyl significantly reduced the number of cysteine residues accessible to 5,5'-dithiobis-(2-nitrobenzoic acid); there were 4.77 +/- 0.21 and 3.49 +/- 0.35 residues accessible per tubulin dimer in the presence of 50 and 100 microM benomyl respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsicum*
  • Dithionitrobenzoic Acid / metabolism
  • Indicators and Reagents / pharmacology
  • Plant Proteins / chemistry*
  • Plant Proteins / metabolism*
  • Protein Multimerization / drug effects
  • Protein Structure, Quaternary
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / metabolism*
  • Temperature
  • Tubulin / chemistry
  • Tubulin / metabolism*

Substances

  • Indicators and Reagents
  • Plant Proteins
  • Recombinant Proteins
  • Tubulin
  • Dithionitrobenzoic Acid