Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation

Investor logo

Warning

This publication doesn't include Institute of Computer Science. It includes Faculty of Medicine. Official publication website can be found on muni.cz.
Authors

DAS Debabrata TRIVEDI Shalini BLAŽÍČKOVÁ Jitka ARUR Swathi SILVA Nicola

Year of publication 2022
Type Article in Periodical
Magazine / Source G3-Genes, Genomes, Genetics
MU Faculty or unit

Faculty of Medicine

Citation
Web https://academic.oup.com/g3journal/article/12/5/jkac079/6564663?login=true
Doi http://dx.doi.org/10.1093/g3journal/jkac079
Keywords Caenorhabditis elegans meiosis; HORMA-domain proteins; HTP-3
Description Generation of functional gametes is accomplished through a multilayered and finely orchestrated succession of events during meiotic progression. In the Caenorhabditis elegans germline, the HORMA-domain-containing protein HTP-3 plays pivotal roles for the establishment of chromosome axes and the efficient induction of programmed DNA double-strand breaks, both of which are crucial for crossover formation. Double-strand breaks allow for accurate chromosome segregation during the first meiotic division and therefore are an essential requirement for the production of healthy gametes. Phosphorylation-dependent regulation of HORMAD protein plays important roles in controlling meiotic chromosome behavior. Here, we document a phospho-site in HTP-3 at Serine 285 that is constitutively phosphorylated during meiotic prophase I. pHTP-3(S285) localization overlaps with panHTP-3 except in nuclei undergoing physiological apoptosis, in which pHTP-3 is absent. Surprisingly, we observed that phosphorylation of HTP-3 at S285 is independent of the canonical kinases that control meiotic progression in nematodes. During meiosis, the htp-3(S285A) mutant displays accelerated RAD-51 turnover, but no other meiotic abnormalities. Altogether, these data indicate that the Ser285 phosphorylation is independent of canonical meiotic protein kinases and does not regulate HTP-3-dependent meiotic processes. We propose a model wherein phosphorylation of HTP-3 occurs through noncanonical or redundant meiotic kinases and/or is likely redundant with additional phospho-sites for function in vivo.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info