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Research Articles

Organ-specific proteomes of Selaginella convoluta provide insights into its desiccation tolerance mechanisms

, , , , , , , , , , , , & ORCID Icon show all
Pages 696-703 | Received 08 Nov 2023, Accepted 02 May 2024, Published online: 16 May 2024
 

Abstract

Selaginella convoluta is a desiccation-tolerant lycophyte capable of enduring water deprivation by arresting its metabolism when dry and reactivating it upon rehydration. Mechanisms to mitigate the harmful effects of desiccation have been investigated in an evolutionary context; however, plants have additional species-specific strategies refined by environmental conditions. Previous metabolome analysis pointed out S. convoluta as a source of chemodiversity. Shotgun proteomic analysis, conducted using an Orbitrap Elite and analyzed with PatternLab for proteomics, compared shoots and roots under two hydration conditions. Our approach identified 1,176 proteins. Proteins associated with photosynthesis, stress, and defense (primarily Reactive Oxygen Species scavengers and chaperones) were enriched in the shoots’ proteome in both hydrated and desiccated states. Post-hydration, roots exhibited exclusive proteins involved in defense, metabolism, and protein trafficking (notably 14-3-3-like proteins, and a putative Bet_v_1 domain-containing protein, which was 15.6 times more abundant in dehydrated roots). These results demonstrate that S. convoluta, when harvested in its dried state from its natural habitat, serves as a valuable source of molecular data, reflecting a realistic multifactorial environmental scenario.

Acknowledgments

The authors acknowledge George Stephenson Batista, manager of the Ecological Station of Seridó, Edweslley Otaviano de Moura that located this pteridophyte in the Brazilian semiarid, and Letícia Gondim Lambert Moreira for the drawing of the representative figure of Selaginella convoluta in its dehydrated state.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Data availability statement

The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE (Vizcaíno et al. Citation2012) partner repository with the dataset identifier PXD024523.

Additional information

Funding

This research was funded by the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior – Brazil (CAPES-Finance Code 001), by the Ministry of Science, Technology, Innovation and Communications – MCTIC, CNPq/National Council of Science and Technology – INCT BioNat, [grant number 465637/2014-0], São Paulo Research Foundation (FAPESP grant INCTBioNat 2014/50926-0), and by Financiadora de Estudos e Projetos (FINEP −0172/18 of M.V.S).

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