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...

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Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 45(2007), 12 vom: 15. Dez., Seite 867-77
1. Verfasser: Stoppin-Mellet, Virginie (VerfasserIn)
Weitere Verfasser: Gaillard, Jérémie, Timmers, Ton, Neumann, Emmanuelle, Conway, James, Vantard, Marylin
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
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 Katanin
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245 1 0 |a Arabidopsis katanin binds microtubules using a multimeric microtubule-binding domain 
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520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a DNA Primers  |2 NLM 
650 7 |a DNA, Plant  |2 NLM 
650 7 |a Recombinant Fusion Proteins  |2 NLM 
650 7 |a Adenosine Triphosphatases  |2 NLM 
650 7 |a EC 3.6.1.-  |2 NLM 
650 7 |a KTN1 protein, Arabidopsis  |2 NLM 
650 7 |a EC 5.6.1.1  |2 NLM 
650 7 |a Katanin  |2 NLM 
650 7 |a EC 5.6.1.1  |2 NLM 
700 1 |a Gaillard, Jérémie  |e verfasserin  |4 aut 
700 1 |a Timmers, Ton  |e verfasserin  |4 aut 
700 1 |a Neumann, Emmanuelle  |e verfasserin  |4 aut 
700 1 |a Conway, James  |e verfasserin  |4 aut 
700 1 |a Vantard, Marylin  |e verfasserin  |4 aut 
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