title: C-sequence of the Dictyostelium cytoplasmic dynein participates in processivity modulation.
abstract: We examined the functional roles of C-sequence, a 47-kDa non-AAA+ module at the C-terminal end of the 380-kDa Dictyostelium dynein motor domain. When the distal segment of the C-sequence was deleted from the motor domain, the single-molecule processivity of the dimerized motor domain was selectively impaired without its ensemble motile ability and ATPase activity being severely affected. When the hinge-like sequence between the distal and proximal C-sequence segments was made more or less flexible, the dimeric motor showed lower or higher processivity, respectively. These results suggest a potential function of the distal C-sequence segment as a modulator of processivity.
authors.affiliation: Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo, Japan.
authors.forename: Naoki
authors.initials: N
authors.lastname: Numata
authors.forename: Tomohiro
authors.initials: T
authors.lastname: Shima
authors.forename: Reiko
authors.initials: R
authors.lastname: Ohkura
authors.forename: Takahide
authors.initials: T
authors.lastname: Kon
authors.forename: Kazuo
authors.initials: K
authors.lastname: Sutoh
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D056445:Cytoplasmic Dyneins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004023:Dictyostelium / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017386:Sequence Homology, Amino Acid
chemical_list: D000255:Adenosine Triphosphate; D056445:Cytoplasmic Dyneins