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© The Rockefeller University Press, 0021-9525/1997//957 $5.00
The Journal of Cell Biology, Volume 136, Number 5, , 1997 957-967

Article

The Yeast Red1 Protein Localizes to the Cores of Meiotic Chromosomes



Albert V. Smith and G. Shirleen Roeder

Department of Biology, Yale University, New Haven, Connecticut 06520-8103

Mutants in the meiosis-specific RED1 gene of S. cerevisiae fail to make any synaptonemal complex (SC) or any obvious precursors to the SC. Using antibodies that specifically recognize the Red1 protein, Red1 has been localized along meiotic pachytene chromosomes. Red1 also localizes to the unsynapsed axial elements present in a zip1 mutant, suggesting that Red1 is a component of the lateral elements of mature SCs. Anti-Red1 staining is confined to the cores of meiotic chromosomes and is not associated with the loops of chromatin that lie outside the SC. Analysis of the spo11 mutant demonstrates that Red1 localization does not depend upon meiotic recombination. The localization of Red1 has been compared with two other meiosisspecific components of chromosomes, Hop1 and Zip1; Zip1 serves as a marker for synapsed chromosomes. Double labeling of wild-type meiotic chromosomes with anti-Zip1 and anti-Red1 antibodies demonstrates that Red1 localizes to chromosomes both before and during pachytene. Double labeling with anti-Hop1and anti-Red1 antibodies reveals that Hop1 protein localizes only in areas that also contain Red1, and studies of Hop1 localization in a red1 null mutant demonstrate that Hop1 localization depends on Red1 function. These observations are consistent with previous genetic studies suggesting that Red1 and Hop1 directly interact. There is little or no Hop1 protein on pachytene chromosomes or in synapsed chromosomal regions.

Please address all correspondence to G.S Roeder, Department of Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103. Tel.: (203) 432-3501. Fax: (203) 432-3263. E-Mail: shirleen.roeder{at}yale.edu

1. Abbreviation used in this paper: SC, synaptonemal complex.


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