Dataset Information

Proteome Dynamics of the Cotyledonary Haustorium and Endosperm in the Course of Germination of Euterpe oleracea Seeds

ABSTRACT: The role of the cotyledonary haustorium (CH) in the mobilization of nutrient reserves in the endosperm of species of the palm family Arecaceae is a moot question. To shed light on this matter, we present here an analysis of the quantitative proteome changes associated with four developmental stages of CH and three of endosperm during germination. Together, a total of 1965 proteins were identified, being 1538 in the CH and 960 in the endosperm. Both in the CH and endosperm proteomes, we observed an increase in the diversity of hydrolases as the CH and endosperm develops. Qualitative proteomics analysis of four CH developmental stages indicated that each stage is populated by a unique set of proteins and the quantitative analysis data showed an increase in the relative abundance of hydrolases, particularly mannan degrading enzymes, as development progresses. These results add weight to the hypothesis that the CH in the seeds of E. oleracea acts both as a conduit of carbon and nitrogen sources generated by the hydrolysis of the reserves in the endosperm and as a source of hydrolases that will contribute to the mobilization of these reserves.

INSTRUMENT(S): LTQ Orbitrap Velos, Q Exactive

ORGANISM(S): Euterpe Oleracea

TISSUE(S): Cotyledon, Endosperm

SUBMITTER: Proteomics Unit

LAB HEAD: Fabio Nogueira

PROVIDER: PXD017481 | Pride | 2021-01-27

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

Items per page:

1 - 5 of 66

Publications

Proteome dynamics of the cotyledonary haustorium and endosperm in the course of germination of Euterpe oleracea seeds.

Nascimento José R S JRS Neto Domingos F DF Coutinho Ítalo C ÍC Domont Gilberto B GB Nogueira Fábio C S FCS Campos Francisco A P FAP

Plant science : an international journal of experimental plant biology 20200618

The role of the cotyledonary haustorium (CH) in the mobilization of nutrient reserves in the endosperm of species of the palm family Arecaceae is a moot question. To shed light on this matter, we present here an analysis of the quantitative proteome changes associated with four developmental stages of CH and three of endosperm during germination. Together, a total of 1965 proteins were identified, being 1538 in the CH and 960 in the endosperm. Both in the CH and endosperm proteomes, we observed ...[more]

PMID: 32771170

Similar Datasets

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
	Acai_endosperma.msf	Msf
	HAUS_FINAL-01.msf	Msf
	QE-002935_Roberto_E1B1-A.raw	Raw
	QE-002936_Roberto_E1B1-B.raw	Raw
	QE-002937_Roberto_E1B1-C.raw	Raw