Comparative qualitative phosphoproteomics analysis identifies shared phosphorylation motifs and associated biological processes in evolutionary divergent plants

Al-Momani, Shireen, Qi, Da ORCID: 0000-0001-6079-9764, Ren, Zhe and Jones, Andrew R ORCID: 0000-0001-6118-9327 (2018) Comparative qualitative phosphoproteomics analysis identifies shared phosphorylation motifs and associated biological processes in evolutionary divergent plants. JOURNAL OF PROTEOMICS, 181. pp. 152-159.

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Abstract

Phosphorylation is one of the most prevalent post-translational modifications and plays a key role in regulating cellular processes. We carried out a bioinformatics analysis of pre-existing phosphoproteomics data, to profile two model species representing the largest subclasses in flowering plants the dicot Arabidopsis thaliana and the monocot Oryza sativa, to understand the extent to which phosphorylation signaling and function is conserved across evolutionary divergent plants. We identified 6537 phosphopeptides from 3189 phosphoproteins in Arabidopsis and 2307 phosphopeptides from 1613 phosphoproteins in rice. We identified phosphorylation motifs, finding nineteen pS motifs and two pT motifs shared in rice and Arabidopsis. The majority of shared motif-containing proteins were mapped to the same biological processes with similar patterns of fold enrichment, indicating high functional conservation. We also identified shared patterns of crosstalk between phosphoserines with enrichment for motifs pSXpS, pSXXpS and pSXXXpS, where X is any amino acid. Lastly, our results identified several pairs of motifs that are significantly enriched to co-occur in Arabidopsis proteins, indicating cross-talk between different sites, but this was not observed in rice.

Item Type:	Article
Uncontrolled Keywords:	Bioinformatics, Phosphoproteomics, Motif identification, Evolutionary conservation, Pathway analysis
Depositing User:	Symplectic Admin
Date Deposited:	08 Feb 2019 16:12
Last Modified:	19 Jan 2023 01:04
DOI:	10.1016/j.jprot.2018.04.011
Open Access URL:	https://doi.org/10.1016/j.jprot.2018.04.011
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3032545