Cargando…
Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis
In Saccharomyces cerevisiae, the mother cell and bud are connected by a narrow neck. The mechanism by which this neck is closed during cytokinesis has been unclear. Here we report on the role of a contractile actomyosin ring in this process. Myo1p (the only type II myosin in S. cerevisiae) forms a r...
Autores principales: | , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1998
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2149343/ https://www.ncbi.nlm.nih.gov/pubmed/9732290 |
_version_ | 1782144538291208192 |
---|---|
author | Bi, Erfei Maddox, Paul Lew, Daniel J. Salmon, E.D. McMillan, John N. Yeh, Elaine Pringle, John R. |
author_facet | Bi, Erfei Maddox, Paul Lew, Daniel J. Salmon, E.D. McMillan, John N. Yeh, Elaine Pringle, John R. |
author_sort | Bi, Erfei |
collection | PubMed |
description | In Saccharomyces cerevisiae, the mother cell and bud are connected by a narrow neck. The mechanism by which this neck is closed during cytokinesis has been unclear. Here we report on the role of a contractile actomyosin ring in this process. Myo1p (the only type II myosin in S. cerevisiae) forms a ring at the presumptive bud site shortly before bud emergence. Myo1p ring formation depends on the septins but not on F-actin, and preexisting Myo1p rings are stable when F-actin is depolymerized. The Myo1p ring remains in the mother–bud neck until the end of anaphase, when a ring of F-actin forms in association with it. The actomyosin ring then contracts to a point and disappears. In the absence of F-actin, the Myo1p ring does not contract. After ring contraction, cortical actin patches congregate at the mother–bud neck, and septum formation and cell separation rapidly ensue. Strains deleted for MYO1 are viable; they fail to form the actin ring but show apparently normal congregation of actin patches at the neck. Some myo1Δ strains divide nearly as efficiently as wild type; other myo1Δ strains divide less efficiently, but it is unclear whether the primary defect is in cytokinesis, septum formation, or cell separation. Even cells lacking F-actin can divide, although in this case division is considerably delayed. Thus, the contractile actomyosin ring is not essential for cytokinesis in S. cerevisiae. In its absence, cytokinesis can still be completed by a process (possibly localized cell–wall synthesis leading to septum formation) that appears to require septin function and to be facilitated by F-actin. |
format | Text |
id | pubmed-2149343 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1998 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21493432008-05-01 Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis Bi, Erfei Maddox, Paul Lew, Daniel J. Salmon, E.D. McMillan, John N. Yeh, Elaine Pringle, John R. J Cell Biol Articles In Saccharomyces cerevisiae, the mother cell and bud are connected by a narrow neck. The mechanism by which this neck is closed during cytokinesis has been unclear. Here we report on the role of a contractile actomyosin ring in this process. Myo1p (the only type II myosin in S. cerevisiae) forms a ring at the presumptive bud site shortly before bud emergence. Myo1p ring formation depends on the septins but not on F-actin, and preexisting Myo1p rings are stable when F-actin is depolymerized. The Myo1p ring remains in the mother–bud neck until the end of anaphase, when a ring of F-actin forms in association with it. The actomyosin ring then contracts to a point and disappears. In the absence of F-actin, the Myo1p ring does not contract. After ring contraction, cortical actin patches congregate at the mother–bud neck, and septum formation and cell separation rapidly ensue. Strains deleted for MYO1 are viable; they fail to form the actin ring but show apparently normal congregation of actin patches at the neck. Some myo1Δ strains divide nearly as efficiently as wild type; other myo1Δ strains divide less efficiently, but it is unclear whether the primary defect is in cytokinesis, septum formation, or cell separation. Even cells lacking F-actin can divide, although in this case division is considerably delayed. Thus, the contractile actomyosin ring is not essential for cytokinesis in S. cerevisiae. In its absence, cytokinesis can still be completed by a process (possibly localized cell–wall synthesis leading to septum formation) that appears to require septin function and to be facilitated by F-actin. The Rockefeller University Press 1998-09-07 /pmc/articles/PMC2149343/ /pubmed/9732290 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Bi, Erfei Maddox, Paul Lew, Daniel J. Salmon, E.D. McMillan, John N. Yeh, Elaine Pringle, John R. Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis |
title | Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis |
title_full | Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis |
title_fullStr | Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis |
title_full_unstemmed | Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis |
title_short | Involvement of an Actomyosin Contractile Ring in Saccharomyces cerevisiae Cytokinesis |
title_sort | involvement of an actomyosin contractile ring in saccharomyces cerevisiae cytokinesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2149343/ https://www.ncbi.nlm.nih.gov/pubmed/9732290 |
work_keys_str_mv | AT bierfei involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis AT maddoxpaul involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis AT lewdanielj involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis AT salmoned involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis AT mcmillanjohnn involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis AT yehelaine involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis AT pringlejohnr involvementofanactomyosincontractileringinsaccharomycescerevisiaecytokinesis |