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© The Rockefeller University Press, 0021-9525/2000//417 $5.00
The Journal of Cell Biology, Volume 148, Number 3, , 2000 417-426

Original Article

Organization of the Yeast Zip1 Protein within the Central Region of the Synaptonemal Complex



Hengjiang Donga,c and G. Shirleen Roedera,b,c

a Department of Molecular, Cellular and Developmental Biology,
b Department of Genetics, Yale University, New Haven, Connecticut 06520-8103
c Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520-8103
Department of Molecular, Cellular and Developmental Biology, Howard Hughes Medical Institute, Yale University, 219 Prospect Street, P.O. Box 208103, New Haven, CT 06520-8103.(203) 432-3263(203) 432-3501

shirleen.roeder{at}yale.edu

The yeast Zip1 protein is a component of the central region of the synaptonemal complex (SC). Zip1 is predicted to form an {alpha}-helical coiled coil, flanked by globular domains at the NH2 and COOH termini. Immunogold labeling with domain-specific anti–Zip1 antibodies demonstrates that the NH2-terminal domain of Zip1 is located in the middle of the central region of the SC, whereas the COOH-terminal domain is embedded in the lateral elements of the complex. Previous studies have shown that overproduction of Zip1 results in the assembly of two types of aggregates, polycomplexes and networks, that are unassociated with chromatin. Our epitope mapping data indicate that the organization of Zip1 within polycomplexes is similar to that of the SC, whereas the organization of Zip1 within networks is fundamentally different. Zip1 protein purified from bacteria assembles into dimers in vitro, and electron microscopic analysis demonstrates that the two monomers within a dimer are arranged in parallel and in register. Together, these results suggest that two Zip1 dimers, lying head-to-head, span the width of the SC.

Key Words: Saccharomyces cerevisiae • meiosis • chromosome synapsis • transverse filament • polycomplex

© 2000 The Rockefeller University Press

Abbreviations used in this paper: EM, electron microscope; GST, glutathione-S-transferase; SC, synaptonemal complex; 6xHis, hexamer of histidine residues.


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