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Proteomics of cassava storage roots before and after shoot pruning

ABSTRACT: Cassava (Manihot esculenta Crantz) is a food security crop for approximately 800 million people, primarily in developing economies. Cassava root yield is determined by the allocation of photoassimilated carbon within the plant, yet there is limited molecular and biochemical information about source-sink relationships in this globally important crop. Here we conducted label free protein quantification using proteomics of Cassava roots before pruning (0 DAP) and 10 days after pruning (10 DAP). This dataset complements transcriptomics analyses and metabolomics analyses described in the associated publication by David et al.

INSTRUMENT(S):

ORGANISM(S): Manihot Esculenta (cassava) (jatropha Manihot)

TISSUE(S): Plant Cell, Root

SUBMITTER: Barbara Pfister

LAB HEAD: Samuel Christian Zeeman

PROVIDER: PXD045690 | Pride | 2026-04-01

REPOSITORIES: Pride

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Project description:Hordeum vulgare (barley) hordoindolines (HINs), HINa, HINb1 and HINb2, are orthologous proteins of wheat puroindolines (PINs) that are small, basic, cysteine-rich seed-specific proteins and responsible for grain hardness. Grain hardness, is, next to its protein content, a major quality trait. In barley, HINb is most highly expressed in the mid-stage developed endosperm and is associated with both major endosperm texture and grain hardness. However, data required tounderstand the spatio-temporal dynamics of HIN transcripts and HIN protein regulation during grain filling processes are missing. Using reverse transcription quantitative PCR (RT-qPCR) and proteomics we analyzed HIN transcript and HIN protein abundance from whole seeds (WSs) at four ((6 days after pollination (dap), 10 dap, 12 dap and ≥ 20 dap)) as well as from aleurone, subaleurone and starchy endosperm at two (12 dap and ≥ 20 dap) developmental stages. At the WS level, results from RT-qPCR, proteomics and western blot showed a continuous increase of HIN transcript and HIN protein abundance across these four developmental stages. Miroscopic studies revealed HIN localization mainly at the vacuolar membrane in the aleurone, at protein bodies (PBs) in subaleurone and at the periphery of starch granules in the starchy endosperm. Laser microdissetion (LMD) proteomic analyses identified HINb2 as the most prominent HIN protein in starchy endosperm at ≥ 20 dap. Additionally, our quantification data revealed a poor correlation between transcript and protein levels of HINs in subaleurone during development. Here, we correlated data achieved by RT-qPCR, proteomics and microscopy that reveal different expression and localization pattern of HINs in each layer during barley endosperm development. This indicats a contribution of each tissue to the regulation of HINs during grain filling. The effect of the high protein abundance of HINs in the starchy endosperm and their localization at the periphery of starch granules at late development stages at the high end-product quality is discussed. Understanding the spatio-temporal regulated HINs is essential to improve barley quality traits for high end-product quality, as hard texture of the barley grain is regulated by the ratio between HINb/HINa.

			Action	DRS
	20111003_100_AA13.RAW	Raw
	20111003_101_B13.RAW	Raw
	20111003_102_AB13.RAW	Raw
	20111003_103_C13.RAW	Raw
	20111003_104_AC13.RAW	Raw

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Proteomics of cassava storage roots before and after shoot pruning

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