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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15 February 1995
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February 15 1995
Zip1-induced changes in synaptonemal complex structure and polycomplex assembly.
M Sym,
M Sym
Department of Biology, Yale University, New Haven, Connecticut 06520-8103.
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G S Roeder
G S Roeder
Department of Biology, Yale University, New Haven, Connecticut 06520-8103.
Search for other works by this author on:
M Sym
Department of Biology, Yale University, New Haven, Connecticut 06520-8103.
G S Roeder
Department of Biology, Yale University, New Haven, Connecticut 06520-8103.
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1995) 128 (4): 455–466.
Citation
M Sym, G S Roeder; Zip1-induced changes in synaptonemal complex structure and polycomplex assembly.. J Cell Biol 15 February 1995; 128 (4): 455–466. doi: https://doi.org/10.1083/jcb.128.4.455
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