Journal Highlight: Affinity proteomics reveals extensive phosphorylation of the Brassica chromosome axis protein ASY1 and a network of associated proteins at prophase I of meiosis

Skip to Navigation

Ezine

  • Published: Jan 29, 2018
  • Author: separationsNOW
  • Channels: Proteomics & Genomics
thumbnail image: Journal Highlight: Affinity proteomics reveals extensive phosphorylation of the <em>Brassica</em> chromosome axis protein ASY1 and a network of associated proteins at prophase I of meiosis

Affinity proteomics has been applied to analyse the proteins that are associated with the meiotic chromosome axis protein, ASY1, in Brassica oleracea anthers and meiocytes.

Affinity proteomics reveals extensive phosphorylation of the Brassica chromosome axis protein ASY1 and a network of associated proteins at prophase I of meiosis

The Plant Journal, 2018, 93, 17-33
Kim Osman, Jianhua Yang, Elisabeth Roitinger, Christophe Lambing, Stefan Heckmann, Elaine Howell, Maria Cuacos, Richard Imre, Gerhard Dürnberger, Karl Mechtler, Susan Armstrong and F. Christopher H. Franklin

Abstract: During meiosis, the formation of crossovers (COs) generates genetic variation and provides physical links that are essential for accurate chromosome segregation. COs occur in the context of a proteinaceous chromosome axis. The transcriptomes and proteomes of anthers and meiocytes comprise several thousand genes and proteins, but because of the level of complexity relatively few have been functionally characterized. Our understanding of the physical and functional interactions between meiotic proteins is also limited. Here we use affinity proteomics to analyse the proteins that are associated with the meiotic chromosome axis protein, ASY1, in Brassica oleracea anthers and meiocytes. We show that during prophase I ASY1 and its interacting partner, ASY3, are extensively phosphorylated, and we precisely assign phosphorylation sites. We identify 589 proteins that co-immunoprecipitate with ASY1. These correspond to 492 Arabidopsis orthologues, over 90% of which form a coherent protein–protein interaction (PPI) network containing known and candidate meiotic proteins, including proteins more usually associated with other cellular processes such as DNA replication and proteolysis. Mutant analysis confirms that affinity proteomics is a viable strategy for revealing previously unknown meiotic proteins, and we show how the PPI network can be used to prioritise candidates for analysis. Finally, we identify another axis-associated protein with a role in meiotic recombination. Data are available via ProteomeXchange with identifier PXD006042.

  • This paper is free to view for all users registered on separationsNOW.com until the end of April 2018.
    After this time, you can purchase it using Pay-Per-View on Wiley Online Library.

Follow us on Twitter!

Social Links

Share This Links

Bookmark and Share

Microsites

Suppliers Selection
Societies Selection

Banner Ad

Click here to see
all job opportunities

Copyright Information

Interested in spectroscopy? Visit our sister site spectroscopyNOW.com

Copyright © 2018 John Wiley & Sons, Inc. All Rights Reserved