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Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation
Tropomyosin is a coiled-coil protein that binds and regulates actin filaments. The tropomyosin gene in Schizosaccharomyces pombe, cdc8, is required for formation of actin cables, contractile rings, and polar localization of actin patches. The roles of conserved residues were investigated in gene rep...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542287/ https://www.ncbi.nlm.nih.gov/pubmed/26187949 http://dx.doi.org/10.1242/bio.012609 |
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author | Cranz-Mileva, Susanne MacTaggart, Brittany Russell, Jacquelyn Hitchcock-DeGregori, Sarah E. |
author_facet | Cranz-Mileva, Susanne MacTaggart, Brittany Russell, Jacquelyn Hitchcock-DeGregori, Sarah E. |
author_sort | Cranz-Mileva, Susanne |
collection | PubMed |
description | Tropomyosin is a coiled-coil protein that binds and regulates actin filaments. The tropomyosin gene in Schizosaccharomyces pombe, cdc8, is required for formation of actin cables, contractile rings, and polar localization of actin patches. The roles of conserved residues were investigated in gene replacement mutants. The work validates an evolution-based approach to identify tropomyosin functions in living cells and sites of potential interactions with other proteins. A cdc8 mutant with near-normal actin affinity affects patch polarization and vacuole fusion, possibly by affecting Myo52p, a class V myosin, function. The presence of labile residual cell attachments suggests a delay in completion of cell division and redistribution of cell patches following cytokinesis. Another mutant with a mild phenotype is synthetic negative with GFP-fimbrin, inferring involvement of the mutated tropomyosin sites in interaction between the two proteins. Proteins that assemble in the contractile ring region before actin do so in a mutant cdc8 strain that cannot assemble condensed actin rings, yet some cells can divide. Of general significance, LifeAct-GFP negatively affects the actin cytoskeleton, indicating caution in its use as a biomarker for actin filaments. |
format | Online Article Text |
id | pubmed-4542287 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Company of Biologists |
record_format | MEDLINE/PubMed |
spelling | pubmed-45422872015-09-16 Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation Cranz-Mileva, Susanne MacTaggart, Brittany Russell, Jacquelyn Hitchcock-DeGregori, Sarah E. Biol Open Research Article Tropomyosin is a coiled-coil protein that binds and regulates actin filaments. The tropomyosin gene in Schizosaccharomyces pombe, cdc8, is required for formation of actin cables, contractile rings, and polar localization of actin patches. The roles of conserved residues were investigated in gene replacement mutants. The work validates an evolution-based approach to identify tropomyosin functions in living cells and sites of potential interactions with other proteins. A cdc8 mutant with near-normal actin affinity affects patch polarization and vacuole fusion, possibly by affecting Myo52p, a class V myosin, function. The presence of labile residual cell attachments suggests a delay in completion of cell division and redistribution of cell patches following cytokinesis. Another mutant with a mild phenotype is synthetic negative with GFP-fimbrin, inferring involvement of the mutated tropomyosin sites in interaction between the two proteins. Proteins that assemble in the contractile ring region before actin do so in a mutant cdc8 strain that cannot assemble condensed actin rings, yet some cells can divide. Of general significance, LifeAct-GFP negatively affects the actin cytoskeleton, indicating caution in its use as a biomarker for actin filaments. The Company of Biologists 2015-07-17 /pmc/articles/PMC4542287/ /pubmed/26187949 http://dx.doi.org/10.1242/bio.012609 Text en © 2015. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Cranz-Mileva, Susanne MacTaggart, Brittany Russell, Jacquelyn Hitchcock-DeGregori, Sarah E. Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
title | Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
title_full | Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
title_fullStr | Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
title_full_unstemmed | Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
title_short | Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
title_sort | evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542287/ https://www.ncbi.nlm.nih.gov/pubmed/26187949 http://dx.doi.org/10.1242/bio.012609 |
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