Journal
DEVELOPMENTAL CELL
Volume 10, Issue 6, Pages 809-819Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2006.04.003
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Funding
- NIGMS NIH HHS [GM28904] Funding Source: Medline
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We have characterized Zip4 (a.k.a. Spo22), a melosisspecific protein essential for chromosome synapsis in budding yeast. In the absence of Zip4, the synaptonernal complex protein Zip1 fails to polymerize along chromosomes. Zip2 and Zip3 are previously characterized components of the synapsis initiation complex. Zip4 forms a functional unit with Zip2 that is distinct from Zip3. Zip2 and Zip4 are mutually dependent for their chromosomal localization; in polycomplexes, the pattern of Zip2/Zip4 localization is distinct from that of Zip3. Crossing-over is decreased in the zip4 mutant (as in zip1, zip2, and zip3); the remaining crossovers are largely dependent on a parallel pathway utilizing Mms4. zip4 displays a novel phenotype: negative crossover interference, meaning that crossovers tend to cluster. This clustering depends on Zip1. Our results suggest an interaction between crossover pathways such that a protein (Zip1) acting in one pathway influences the distribution of crossovers promoted by a parallel (Mms4-dependent) pathway.
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