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Dam1 complex-microtubule interaction

ABSTRACT: we used cross-linking mass spectrometry to determine the molecular architecture of the Dam1 complex alone and bound to microtubules. Our data provide a map of the subunit arrangement of the Dam1 complex. Analysis of the Dam1 complex assembled around microtubules reveals that the Spc34 and Ask1 subunits are likely involved in self -assembly whereas the Duo1 and Dam1 subunits both interact with microtubules. We also demonstrate that the C termini of Dam1 and Duo1 provide the microtubule binding properties to the Dam1 complex. Our data provides key information on the organization of the Dam1 complex around microtubules.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Candida Albicans (yeast)

SUBMITTER: Juan Zou

LAB HEAD: Prof. Juri Rappsilber

PROVIDER: PXD003678 | Pride | 2016-03-01

REPOSITORIES: Pride

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			Action	DRS
	Dam1.txt	Txt
	Dam1_Duo1Short.txt	Txt
	Dam1_MT.txt	Txt
	Zou_Rappsilber_JW_Dam1MT_BS3_2015.raw	Raw
	Zou_Rappsilber_JW_Dam1MT_BS3_2015.xlsx	Xlsx

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Publications

Molecular architecture of the Dam1 complex-microtubule interaction.

Legal Thibault T Zou Juan J Sochaj Alicja A Rappsilber Juri J Welburn Julie P I JP

Open biology 20160301 3

Mitosis is a highly regulated process that allows the equal distribution of the genetic material to the daughter cells. Chromosome segregation requires the formation of a bipolar mitotic spindle and assembly of a multi-protein structure termed the kinetochore to mediate attachments between condensed chromosomes and spindle microtubules. In budding yeast, a single microtubule attaches to each kinetochore, necessitating robustness and processivity of this kinetochore-microtubule attachment. The ye ...[more]

PMID: 26962051

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