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Key residues on microtubule responsible for activation of kinesin ATPase.
Uchimura, Seiichi; Oguchi, Yusuke; Hachikubo, You; Ishiwata, Shin'ichi; Muto, Etsuko.
Afiliação
  • Uchimura S; Laboratory for Molecular Biophysics, Brain Science Institute, RIKEN, Wako, Saitama, Japan. uchimura@brain.riken.jp
EMBO J ; 29(7): 1167-75, 2010 Apr 07.
Article em En | MEDLINE | ID: mdl-20224548
Microtubule (MT) binding accelerates the rate of ATP hydrolysis in kinesin. To understand the underlying mechanism, using charged-to-alanine mutational analysis, we identified two independent sites in tubulin, which are critical for kinesin motility, namely, a cluster of negatively charged residues spanning the helix 11-12 (H11-12) loop and H12 of alpha-tubulin, and the negatively charged residues in H12 of beta-tubulin. Mutation in the alpha-tubulin-binding site results in a deceleration of ATP hydrolysis (k(cat)), whereas mutation in the beta-tubulin-binding site lowers the affinity for MTs (K(0.5)MT). The residue E415 in alpha-tubulin seems to be important for coupling MT binding and ATPase activation, because the mutation at this site results in a drastic reduction in the overall rate of ATP hydrolysis, largely due to a deceleration in the reaction of ADP release. Our results suggest that kinesin binding at a region containing alpha-E415 could transmit a signal to the kinesin nucleotide pocket, triggering its conformational change and leading to the release of ADP.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Tubulina (Proteína) / Cinesinas / Proteínas de Saccharomyces cerevisiae / Microtúbulos Idioma: En Ano de publicação: 2010 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Tubulina (Proteína) / Cinesinas / Proteínas de Saccharomyces cerevisiae / Microtúbulos Idioma: En Ano de publicação: 2010 Tipo de documento: Article