Arabidopsis katanin binds microtubules using a multimeric microtubule-binding domain
Katanin is a heterodimeric protein that mediates ATP-dependent destabilization of microtubules in animal cells. In plants, the catalytic subunit of Arabidopsis thaliana katanin (AtKSS, Arabidopsis thaliana Katanin Small Subunit) has been identified and its microtubule-severing activity has been demo...
Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 45(2007), 12 vom: 15. Dez., Seite 867-77 |
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1. Verfasser: | |
Weitere Verfasser: | , , , , |
Format: | Aufsatz |
Sprache: | English |
Veröffentlicht: |
2007
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Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins DNA Primers DNA, Plant Recombinant Fusion Proteins Adenosine Triphosphatases EC 3.6.1.- KTN1 protein, Arabidopsis EC 5.6.1.1 |
Zusammenfassung: | Katanin is a heterodimeric protein that mediates ATP-dependent destabilization of microtubules in animal cells. In plants, the catalytic subunit of Arabidopsis thaliana katanin (AtKSS, Arabidopsis thaliana Katanin Small Subunit) has been identified and its microtubule-severing activity has been demonstrated in vitro. In vivo, plant katanin plays a role in the organization of cortical microtubules, but the way it achieves this function is unknown. To go further in our understanding of the mechanisms by which katanin severs microtubules, we analyzed the functional domains of Arabidopsis katanin. We characterized the microtubule-binding domain of katanin both in vitro and in vivo. It corresponds to a poorly conserved sequence between plant and animal katanins that is located in the N-terminus of the protein. This domain interacts with cortical microtubules in vivo and has a low affinity for microtubules in vitro. We also observed that katanin microtubule-binding domain oligomerizes into trimers. These results show that, besides being involved in the interaction of katanin with microtubules, the microtubule-binding domain may also participate in the oligomerization of katanin. At the structural level, we observed that AtKSS forms ring-shaped oligomers |
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Beschreibung: | Date Completed 27.02.2008 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1873-2690 |