Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins
Abstract Isolated microtubules from cod ( Gadus morhua ) are apparently more stable to colchicine than bovine microtubules. In order to further characterize this difference, the effect of the colchicine analogue 2‐methoxy‐5‐(2,3,4‐trimethoxyphenyl)‐2,4,6‐cyclo heptatrien‐1‐one (MTC) was studied on a...
Published in: | Cell Motility |
---|---|
Main Authors: | , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
1995
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1002/cm.970300207 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcm.970300207 https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.970300207 |
id |
crwiley:10.1002/cm.970300207 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1002/cm.970300207 2024-06-02T08:06:58+00:00 Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins de Pereda, J. M. Wallin, M. Billger, M. Andreu, J. M. 1995 http://dx.doi.org/10.1002/cm.970300207 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcm.970300207 https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.970300207 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Cell Motility volume 30, issue 2, page 153-163 ISSN 0886-1544 journal-article 1995 crwiley https://doi.org/10.1002/cm.970300207 2024-05-03T10:59:05Z Abstract Isolated microtubules from cod ( Gadus morhua ) are apparently more stable to colchicine than bovine microtubules. In order to further characterize this difference, the effect of the colchicine analogue 2‐methoxy‐5‐(2,3,4‐trimethoxyphenyl)‐2,4,6‐cyclo heptatrien‐1‐one (MTC) was studied on assembly, as measured by turbidity and sedimentation analysis, and on polymer morphology. MTC has the advantage to bind fast and reversible to the colchicine binding site of tubulin even at low temperatures. It was found to bind to one site in cod brain tubulin, with affinity (6.5 ± 1.5) × 10 5 M 1 at both low or high temperature, similarly to bovine brain tubulin. However, the effect of the binding differed. At substoichiometric concentrations of MTC bovine brain microtubule assembly was almost completely inhibited, while less effect was seen on the mass of polymerized cod microtubule proteins. A preformed bovine tubulin‐colchicine complex inhibited the assembly of both cod and bovine microtubules at substoichiometric concentrations, but the effect on the assembly of cod microtubules was less. At higher concentrations (5 × 10 −5 to 1 × 10 −3 M), MTC induced a large amount of cold‐stable spirals of cod proteins, whereas abnormal polymers without any defined structure were formed from bovine proteins. Spirals of cod microtubule proteins were only formed in the presence of microtubule associated proteins (MAPs), indicating that the morphological effect of MTC can be modulated by MAPs. The effects of colchicine and MTC differed. At 10 −5 M colchicine no spirals were formed, while at 10 −4 M and 10 −3 M, a mixture of spirals and aggregates was found. The morphology of the spirals differed both from vinblastine spirals and from the spirals previously found when cod microtubule proteins polymerize in the presence of high Ca 2 concentrations. The present data show that even if the colchicine binding site is conserved between many different species, the bindings have different effects which seem to depend on intrinsic ... Article in Journal/Newspaper Gadus morhua Wiley Online Library Cell Motility 30 2 153 163 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Abstract Isolated microtubules from cod ( Gadus morhua ) are apparently more stable to colchicine than bovine microtubules. In order to further characterize this difference, the effect of the colchicine analogue 2‐methoxy‐5‐(2,3,4‐trimethoxyphenyl)‐2,4,6‐cyclo heptatrien‐1‐one (MTC) was studied on assembly, as measured by turbidity and sedimentation analysis, and on polymer morphology. MTC has the advantage to bind fast and reversible to the colchicine binding site of tubulin even at low temperatures. It was found to bind to one site in cod brain tubulin, with affinity (6.5 ± 1.5) × 10 5 M 1 at both low or high temperature, similarly to bovine brain tubulin. However, the effect of the binding differed. At substoichiometric concentrations of MTC bovine brain microtubule assembly was almost completely inhibited, while less effect was seen on the mass of polymerized cod microtubule proteins. A preformed bovine tubulin‐colchicine complex inhibited the assembly of both cod and bovine microtubules at substoichiometric concentrations, but the effect on the assembly of cod microtubules was less. At higher concentrations (5 × 10 −5 to 1 × 10 −3 M), MTC induced a large amount of cold‐stable spirals of cod proteins, whereas abnormal polymers without any defined structure were formed from bovine proteins. Spirals of cod microtubule proteins were only formed in the presence of microtubule associated proteins (MAPs), indicating that the morphological effect of MTC can be modulated by MAPs. The effects of colchicine and MTC differed. At 10 −5 M colchicine no spirals were formed, while at 10 −4 M and 10 −3 M, a mixture of spirals and aggregates was found. The morphology of the spirals differed both from vinblastine spirals and from the spirals previously found when cod microtubule proteins polymerize in the presence of high Ca 2 concentrations. The present data show that even if the colchicine binding site is conserved between many different species, the bindings have different effects which seem to depend on intrinsic ... |
format |
Article in Journal/Newspaper |
author |
de Pereda, J. M. Wallin, M. Billger, M. Andreu, J. M. |
spellingShingle |
de Pereda, J. M. Wallin, M. Billger, M. Andreu, J. M. Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
author_facet |
de Pereda, J. M. Wallin, M. Billger, M. Andreu, J. M. |
author_sort |
de Pereda, J. M. |
title |
Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
title_short |
Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
title_full |
Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
title_fullStr |
Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
title_full_unstemmed |
Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
title_sort |
comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins |
publisher |
Wiley |
publishDate |
1995 |
url |
http://dx.doi.org/10.1002/cm.970300207 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcm.970300207 https://onlinelibrary.wiley.com/doi/pdf/10.1002/cm.970300207 |
genre |
Gadus morhua |
genre_facet |
Gadus morhua |
op_source |
Cell Motility volume 30, issue 2, page 153-163 ISSN 0886-1544 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/cm.970300207 |
container_title |
Cell Motility |
container_volume |
30 |
container_issue |
2 |
container_start_page |
153 |
op_container_end_page |
163 |
_version_ |
1800751978163208192 |