Front Cover: Proteomes and Phosphoproteomes of Anther and Pollen: Availability and Progress

Zhang, Zaibao; Hu, Menghui; Feng, Xiaobing; Gong, An-Dong; Cheng, Lin; Yuan, Hongyu

doi:10.1002/pmic.201770151

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Proteomics

2017

DOI: 10.1002/pmic.201770151

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Front Cover: Proteomes and Phosphoproteomes of Anther and Pollen: Availability and Progress

Zaibao Zhang¹,

Menghui Hu²,

Xiaobing Feng³

et al.

Abstract: DOI: https://doi.org/10.1002/pmic.201600458 Anther proteomics enables the investigation of anther development and progression at the molecular level. As reported by Zaibao Zhang et al. in article number 1600458, an increase in information generated from anther proteomics research has helped in elucidating the molecular mechanisms of anther development, whilst demonstrating a clear agricultural benefit for plant breeding.

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

et al. 2017

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SummaryDuring 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.

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

et al. 2017

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Front Cover: Proteomes and Phosphoproteomes of Anther and Pollen: Availability and Progress

Cited by 1 publication

References 0 publications

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

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

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