Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization

FEBS Letters

Vernos, Isabelle¹  Serrano, Luis²  Westerholm-Parvinen, Ann¹ 

[1] Cell Biology and Cell Biophysics Program, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany;Structural and Computational Biology Program, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany

关键词: Forkhead homology-associated domain;    Xenopus kinesin-like protein 4;    Kinesin-like protein;    UNC104 subfamily;    FHA;    forkhead homology-associated domain;    Xklp4;    Xenopus kinesin-like protein 4;    KLP;    kinesin-like protein;   

DOI  :  10.1016/S0014-5793(00)02310-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

By sequence analysis we show that the U104 domain found in the UNC104 subfamily of kinesins is a forkhead homology-associated domain (FHA). A combination of limited proteolysis, mass spectroscopy, and physicochemical analysis define this domain as a genuine autonomously folding domain. Our data show that the FHA domain is shorter than previously reported since the C-terminal α-helix is not part of its minimum core. Key amino acids postulated to recognize phosphorylated residues are conserved. These data suggest that the kinesin FHA domains are functional domains involved in protein–protein interactions regulated by phosphorylation.

【 授权许可】

Unknown