Identification of a cysteine residue important for the ATPase activity of C. elegans fidgetin homologue.

Abstract:

:Based on the amino acid alignment, Caenorhabditis elegans F32D1.1 was identified to be a homologue of the mammalian fidgetin. We produced and purified the F32D1.1 protein by using a baculovirus-expression system. F32D1.1 has an ATPase activity, which is sensitive to N-ethylmaleimide. Km and Vmax for the ATPase activity of F32D1.1 were estimated to be 0.44 mM and 225 nmol/mg/min, respectively. When the cysteine at the position of 368 was mutated to alanine, the ATPase activity was greatly decreased; Vmax was decreased to one-sixth, while Km remained similar. These results suggest that the unique position of cysteine 368, located immediately downstream of the Walker A motif, plays an important role in the ATP hydrolysis process of C. elegans F32D1.1 protein.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Yakushiji Y,Yamanaka K,Ogura T

doi

10.1016/j.febslet.2004.11.009

keywords:

subject

Has Abstract

pub_date

2004-12-03 00:00:00

pages

191-7

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(04)01371-7

journal_volume

578

pub_type

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