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Zip1-induced changes in synaptonemal complex structure and polycomplex assembly

The yeast Zip1 protein is a component of the synaptonemal complex (SC), which is an elaborate macromolecular structure found along the lengths of chromosomes during meiosis. Mutations that increase the length of the predicted coiled coil region of the Zip1 protein show that Zip1 influences the width...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1995
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199901/
https://www.ncbi.nlm.nih.gov/pubmed/7860625
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description The yeast Zip1 protein is a component of the synaptonemal complex (SC), which is an elaborate macromolecular structure found along the lengths of chromosomes during meiosis. Mutations that increase the length of the predicted coiled coil region of the Zip1 protein show that Zip1 influences the width of the SC. Overexpression of the ZIP1 gene results in the formation of two distinct types of higher order structures that are found in the nucleus, but not associated with chromatin. One of these structures resembles the polycomplexes that have been observed in many organisms and are thought to be aggregates of SC components. The second type of structure, which we have termed "networks," does not resemble any previously identified SC-related structure. Assembly of both polycomplexes and networks can occur independently of the Hop1 or Red1 protein, which are thought to be SC components. Our results demonstrate that Zip1 is a structural component of the central region of the SC. More specifically, we speculate that Zip1 is a component of the transverse filaments that lie perpendicular to the long axis of the complex.
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spelling pubmed-21999012008-05-01 Zip1-induced changes in synaptonemal complex structure and polycomplex assembly J Cell Biol Articles The yeast Zip1 protein is a component of the synaptonemal complex (SC), which is an elaborate macromolecular structure found along the lengths of chromosomes during meiosis. Mutations that increase the length of the predicted coiled coil region of the Zip1 protein show that Zip1 influences the width of the SC. Overexpression of the ZIP1 gene results in the formation of two distinct types of higher order structures that are found in the nucleus, but not associated with chromatin. One of these structures resembles the polycomplexes that have been observed in many organisms and are thought to be aggregates of SC components. The second type of structure, which we have termed "networks," does not resemble any previously identified SC-related structure. Assembly of both polycomplexes and networks can occur independently of the Hop1 or Red1 protein, which are thought to be SC components. Our results demonstrate that Zip1 is a structural component of the central region of the SC. More specifically, we speculate that Zip1 is a component of the transverse filaments that lie perpendicular to the long axis of the complex. The Rockefeller University Press 1995-02-02 /pmc/articles/PMC2199901/ /pubmed/7860625 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
Zip1-induced changes in synaptonemal complex structure and polycomplex assembly
title Zip1-induced changes in synaptonemal complex structure and polycomplex assembly
title_full Zip1-induced changes in synaptonemal complex structure and polycomplex assembly
title_fullStr Zip1-induced changes in synaptonemal complex structure and polycomplex assembly
title_full_unstemmed Zip1-induced changes in synaptonemal complex structure and polycomplex assembly
title_short Zip1-induced changes in synaptonemal complex structure and polycomplex assembly
title_sort zip1-induced changes in synaptonemal complex structure and polycomplex assembly
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199901/
https://www.ncbi.nlm.nih.gov/pubmed/7860625