Characterization of Capsicum annuum Recombinant α- and β-Tubulin.

Bon-Sung Koo; Myung-Hyun Jang; Haechul Park; Hey-Yeon Park; Jin-Wook Han; Yun-Soo Yeo; Sang-Hong Yoon; Soo-Jin Kim; Chang-Muk Lee; Moon-Young Yoon

Abstract  There are several conditions which might modulate polymerization to produce polymers having normal lattice structure. In the absence of 1 mM MgCl2 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 μM concentration increased 23% tubulin assembly. One millimolar CaCl2, ≥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 μM benomyl respectively.

CAPSICUM annuum; TUBULINS; RECOMBINANT DNA; POLYMERIZATION; BENOMYL; NUCLEATION; DIMETHYL sulfoxide; GLYCERIN

Applied Biochemistry & Biotechnology, 2010, Vol 160, Issue 1, p122

0273-2289

Academic Journal

10.1007/s12010-008-8489-4