ArticleProceedings of the National Academy of Sciences of the United States of America2005
Bioinformatic analyses implicate the collaborating meiotic crossover/chiasma proteins Zip2, Zip3, and Spo22/Zip4 in ubiquitin labeling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 83 citations in OpenAlex.
- Rad51, Rad54, and ZMM proteins antagonize the mismatch repair system to promote fertility of budding yeast intraspecies hybrid zygotes.Nucleic acids research · 2025Article
- Meiosis in budding yeast.Genetics · 2023Article
- The Msh5 complex shows homeostatic localization in response to DNA double-strand breaks in yeast meiosis.Frontiers in cell and developmental biology · 2023Article
- Article
- Genomic and Meiotic Changes Accompanying Polyploidization.Plants (Basel, Switzerland) · 2022Review
- The Zip4 protein directly couples meiotic crossover formation to synaptonemal complex assembly.Genes & development · 2022Article
- Cancer genome datamining and functional genetic analysis implicate mechanisms of ATM/ATR dysfunction underpinning carcinogenesis.Communications biology · 2021Article
- Chromosome-autonomous feedback down-regulates meiotic DNA break competence upon synaptonemal complex formation.Genes & development · 2020Article
- Distinct Functions in Regulation of Meiotic Crossovers for DNA Damage Response Clamp Loader Rad24(Rad17) and Mec1(ATR) Kinase.Genetics · 2019Article
- Review
- A Multiprotein Complex Regulates Interference-Sensitive Crossover Formation in Rice.Plant physiology · 2019Article
- The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding.Nucleic acids research · 2019Article
- HEIP1 regulates crossover formation during meiosis in rice.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- SHOC1 is a ERCC4-(HhH)2-like protein, integral to the formation of crossover recombination intermediates during mammalian meiosis.PLoS genetics · 2018Article
- Zinc Transporter Proteins.Neurochemical research · 2018Review
- A meiotic XPF-ERCC1-like complex recognizes joint molecule recombination intermediates to promote crossover formation.Genes & development · 2018Article
- Genome-Wide Transcription During Early Wheat Meiosis Is Independent of Synapsis, Ploidy Level, and theFrontiers in plant science · 2018Article
- Human male infertility and its genetic causes.Reproductive medicine and biology · 2017Review
- Control of meiotic pairing and recombination by chromosomally tethered 26S proteasome.Science (New York, N.Y.) · 2017Article
- Exploiting theMolecular breeding : new strategies in plant improvement · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Zip2 and Zip3 are meiosis-specific proteins that, in collaboration with several partners, act at the sites of crossover-designated, axis-associated recombinational interactions to mediate crossover/chiasma formation. Here, Spo22 (also called Zip4) is identified as a probable functional collaborator of Zip2/3. The molecular roles of Zip2, Zip3, and Spo22/Zip4 are unknown. All three proteins are part of a small evolutionary cohort comprising similar homologs in four related yeasts. Zip3 is shown to contain a RING finger whose structural features most closely match those of known ubiquitin E3s. Further, Zip3 exhibits major domainal homologies to Rad18, a known DNA-binding ubiquitin E3. Also described is an approach to the identification and mapping of repeated protein sequence motifs, Alignment Based Repeat Annotation (ABRA), that we have developed. When ABRA is applied to Zip2 and Spo22/Zip4, they emerge as a 14-blade WD40-like repeat protein and a 22-unit tetratricopeptide repeat protein, respectively. WD40 repeats of Cdc20, Cdh1, and Cdc16 and tetratricopeptide repeats of Cdc16, Cdc23, and Cdc27, all components of the anaphase-promoting complex, are also analyzed. These and other findings suggest that Zip2, Zip3, and Zip4 act together to mediate a process that involves Zip3-mediated ubiquitin labeling, potentially as a unique type of ubiquitin-conjugating complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.