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Mol Biol Cell. 2017 Mar 15;28(6):825-833. doi: 10.1091/mbc.E16-09-0678. Epub 2017 Jan 18.

A Zip3-like protein plays a role in crossover formation in the SC-less meiosis of the protist Tetrahymena.

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Department of Chromosome Biology, University of Vienna, Vienna Biocenter, 1030 Vienna, Austria.
Institute of Molecular Biotechnology of the Austrian Academy of Sciences and.
Research Institute of Molecular Pathology, 1030 Vienna, Austria.
Department of Chromosome Biology, University of Vienna, Vienna Biocenter, 1030 Vienna, Austria


When programmed meiotic DNA double-strand breaks (DSBs) undergo recombinational repair, genetic crossovers (COs) may be formed. A certain level of this is required for the faithful segregation of chromosomes, but the majority of DSBs are processed toward a safer alternative, namely noncrossovers (NCOs), via nonreciprocal DNA exchange. At the crossroads between these two DSB fates is the Msh4-Msh5 (MutSγ) complex, which stabilizes CO-destined recombination intermediates and members of the Zip3/RNF212 family of RING finger proteins, which in turn stabilize MutSγ. These proteins function in the context of the synaptonemal complex (SC) and mainly act on SC-dependent COs. Here we show that in the SC-less ciliate Tetrahymena, Zhp3 (a protein distantly related to Zip3/RNF212), together with MutSγ, is responsible for the majority of COs. This activity of Zhp3 suggests an evolutionarily conserved SC-independent strategy for balancing CO:NCO ratios. Moreover, we report a novel meiosis-specific protein, Sa15, as an interacting partner of Zhp3. Sa15 forms linear structures in meiotic prophase nuclei to which Zhp3 localizes. Sa15 is required for a wild-type level of CO formation. Its linear organization suggests the existence of an underlying chromosomal axis that serves as a scaffold for Zhp3 and other recombination proteins.

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