Abstract
Baquero et al. report the structure of the HAP2 gamete fusion protein of the Chlamydomonas reinhardtii alga, describing key elements required to bridge two opposite-type gametes and drive their fusion. Mutagenesis of these elements confirmed their membrane-interaction function. Additional specific HAP2 protein-protein interaction sites are described as potential fusion controls.
| Original language | English |
|---|---|
| Journal | Structure |
| Volume | 27 |
| Issue number | 1 |
| Pages (from-to) | 113-124.e4 |
| ISSN | 0969-2126 |
| DOIs | |
| Publication status | Published - 02.01.2019 |
Funding
Funding for this project was provided by the European Research Council (ERC) advanced grant CelCelFus (grant number 340371) to F.A.R., as well as recurrent funding from Institut Pasteur and the CNRS. J.F. had a PhD fellowhsip from Ecole Polytechnique AMX. We thank I. Fernandez for technical help and discussion; W.J. Snell for helpful discussions and for testing the effect antibodies against HAP2 on C. reinhardtii gamete fusion in vivo; Ahmed Haouz and staff of the Pasteur crystallogenesis facility as well as the staff of Proxima-1 and -2 at the SOLEIL synchrotron for help during crystallization screening and diffraction data collection. Funding for this project was provided by the European Research Council (ERC) advanced grant CelCelFus (grant number 340371 ) to F.A.R., as well as recurrent funding from Institut Pasteur and the CNRS . J.F. had a PhD fellowhsip from Ecole Polytechnique AMX. We thank I. Fernandez for technical help and discussion; W.J. Snell for helpful discussions and for testing the effect antibodies against HAP2 on C. reinhardtii gamete fusion in vivo; Ahmed Haouz and staff of the Pasteur crystallogenesis facility as well as the staff of Proxima-1 and -2 at the SOLEIL synchrotron for help during crystallization screening and diffraction data collection.
