The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.

The chromodomain protein, Chromator, is localized to chromosomes during interphase; however, during cell division together with other nuclear proteins Chromator redistributes to form a macro molecular spindle matrix complex that embeds the microtubule spindle apparatus. It has been demonstrated that...

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Autores principales:	Changfu Yao, Chao Wang, Yeran Li, Yun Ding, Uttama Rath, Saheli Sengupta, Jack Girton, Kristen M Johansen, Jørgen Johansen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5e24be7210d4479eae21f8391b15bb41
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spelling	oai:doaj.org-article:5e24be7210d4479eae21f8391b15bb412021-11-25T06:06:51ZThe spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.1932-620310.1371/journal.pone.0103855https://doaj.org/article/5e24be7210d4479eae21f8391b15bb412014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25072297/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The chromodomain protein, Chromator, is localized to chromosomes during interphase; however, during cell division together with other nuclear proteins Chromator redistributes to form a macro molecular spindle matrix complex that embeds the microtubule spindle apparatus. It has been demonstrated that the CTD of Chromator is sufficient for localization to the spindle matrix and that expression of this domain alone could partially rescue Chro mutant microtubule spindle defects. Furthermore, the presence of frayed and unstable microtubule spindles during mitosis after Chromator RNAi depletion in S2 cells indicated that Chromator may interact with microtubules. In this study using a variety of biochemical assays we have tested this hypothesis and show that Chromator not only has binding activity to microtubules with a Kd of 0.23 µM but also to free tubulin. Furthermore, we have mapped the interaction with microtubules to a relatively small stretch of 139 amino acids in the carboxy-terminal region of Chromator. This sequence is likely to contain a novel microtubule binding interface since database searches did not find any sequence matches with known microtubule binding motifs.Changfu YaoChao WangYeran LiYun DingUttama RathSaheli SenguptaJack GirtonKristen M JohansenJørgen JohansenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e103855 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Changfu Yao Chao Wang Yeran Li Yun Ding Uttama Rath Saheli Sengupta Jack Girton Kristen M Johansen Jørgen Johansen The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
description	The chromodomain protein, Chromator, is localized to chromosomes during interphase; however, during cell division together with other nuclear proteins Chromator redistributes to form a macro molecular spindle matrix complex that embeds the microtubule spindle apparatus. It has been demonstrated that the CTD of Chromator is sufficient for localization to the spindle matrix and that expression of this domain alone could partially rescue Chro mutant microtubule spindle defects. Furthermore, the presence of frayed and unstable microtubule spindles during mitosis after Chromator RNAi depletion in S2 cells indicated that Chromator may interact with microtubules. In this study using a variety of biochemical assays we have tested this hypothesis and show that Chromator not only has binding activity to microtubules with a Kd of 0.23 µM but also to free tubulin. Furthermore, we have mapped the interaction with microtubules to a relatively small stretch of 139 amino acids in the carboxy-terminal region of Chromator. This sequence is likely to contain a novel microtubule binding interface since database searches did not find any sequence matches with known microtubule binding motifs.
format	article
author	Changfu Yao Chao Wang Yeran Li Yun Ding Uttama Rath Saheli Sengupta Jack Girton Kristen M Johansen Jørgen Johansen
author_facet	Changfu Yao Chao Wang Yeran Li Yun Ding Uttama Rath Saheli Sengupta Jack Girton Kristen M Johansen Jørgen Johansen
author_sort	Changfu Yao
title	The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
title_short	The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
title_full	The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
title_fullStr	The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
title_full_unstemmed	The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
title_sort	spindle matrix protein, chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/5e24be7210d4479eae21f8391b15bb41
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The spindle matrix protein, Chromator, is a novel tubulin binding protein that can interact with both microtubules and free tubulin.

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