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Dimerization properties of a Xenopus lae ... carboxy-terminal stalk fragment
Dimerization properties of a Xenopus laevis kinesin-II carboxy-terminal stalk fragment.
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We have analysed the structural and physical properties of the carboxy-terminal stalk region of a kinesin-II, Xenopus kinesin-like protein 3A/B (Xklp3A/B), which we showed to be essential for heterodimerization in a previous work (De Marco et al., 2001). We expressed the corresponding A-stalk and B-stalk fragments and investigated their modes of interaction by analytical ultracentrifugation (AUC), circular dichroism spectroscopy, denaturation assays and electron microscopy. Co-expression of the A-stalk and B-stalk produced the properly folded, hetero-dimeric coiled coil at high yields. The dimeric nature of the complex was confirmed by AUC. We also found that the isolated A-stalk fragment forms a stable helix by itself and shows a significant tendency towards homodimer and higher-order complex formation. In the absence of the corresponding A-stalk fragment, the isolated B-stalk fragment remains partially unfolded, which suggests that the A-stalk provides a template structure for the B-stalk in order to recompose the complete heterodimeric coiled coil.
De Marco V, De Marco A, Goldie KN, Correia JJ, Hoenger A
EMBO reports
2003-07-01 00:00
4
7
717-22
Amino Acid Sequence,Animals,Calcium-Binding Proteins,Circular Dichroism,Dimerization,Kinesin,Molecular Sequence Data,Muscle Proteins,Peptide Fragments,Protein Conformation,Protein Folding,Ultracentrifugation,Xenopus Proteins,Xenopus laevis,Calcium-Binding Proteins,Muscle Proteins,Peptide Fragments,XKLP3 protein, Xenopus,Xenopus Proteins,xklp3A protein, Xenopus,kinesin-II,Kinesin
European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
EMBO Rep.
1469-221X
10.1038/sj.embor.embor884
embor884
554
True
12835758
