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Characterisation of the free and membrane-associated fractions of the thylakoid lumen proteome in Arabidopsis thaliana

ABSTRACT: In plants chloroplasts, the lumen of the thylakoid membrane houses proteins that are vital for photosynthetic electron transport, including water-splitting at photosystem (PS) II and shuttling of electrons from cytochrome b6f to PSI. Other lumen proteins maintain photosynthetic activity through biogenesis and turnover of PSII complexes. Although all lumen proteins are soluble, these known details have highlighted interactions of some lumen proteins with thylakoid membranes or thylakoid-intrinsic proteins. Meanwhile, the functional details of most lumen proteins, as well as their distribution between the soluble and membrane-associated lumen fractions, remain unknown. The current study isolated the soluble free lumen (FL) and membrane-associated lumen (MAL) fractions from Arabidopsis thaliana, and used gel- and mass spectrometry-based proteomics methods to analyse the contents of each proteome. These results identified lumenal proteins, and clearly distinguished the difference between the FL and MAL proteomes. The most abundant proteins in the FL fraction were involved in PSII assembly and repair, while the MAL proteome was enriched in proteins that support of the oxygen-evolving complex (OEC). Novel proteins, including a new PsbP domain-containing isoform, as well as several novel post-translational modifications and N-termini, are reported, and bi-dimensional separation of the lumen proteome identified several potential multi-protein oligomers in the thylakoid lumen.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Andrea Trotta

LAB HEAD: Eva-Mari Aro

PROVIDER: PXD027229 | Pride | 2021-07-30

REPOSITORIES: Pride

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			Action	DRS
	2D_Lumen_1.msf	Msf
	2D_Lumen_1.mzML	Mzml
	2D_Lumen_1.mzid.gz	Mzid
	2D_Lumen_1.raw	Raw
	2D_Lumen_10.msf	Msf

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Quantification of the ratio between the two PsbO protein isoforms in the thylakoids lumen of Arabidopsis thaliana

Project description:In plants chloroplasts, the lumen of the thylakoid membrane houses proteins that are vital for photosynthetic electron transport, including water-splitting at photosystem (PS) II and shuttling of electrons from cytochrome b6f to PSI. Other lumen proteins maintain photosynthetic activity through biogenesis and turnover of PSII complexes. Although all lumen proteins are soluble, these known details have highlighted interactions of some lumen proteins with thylakoid membranes or thylakoid-intrinsic proteins. Meanwhile, the functional details of most lumen proteins, as well as their distribution between the soluble and membrane-associated lumen fractions, remain unknown. The current study isolated the soluble free lumen (FL) and membrane-associated lumen (MAL) fractions from Arabidopsis thaliana, and used mass spectrometry-based proteomics methods to analyse the contents of each proteome. These results identified lumenal proteins, and clearly distinguished the difference between the FL and MAL proteomes. The most abundant proteins in the FL fraction were involved in PSII assembly and repair, while the MAL proteome was enriched in proteins that support of the oxygen-evolving complex (OEC). Selected Reaction Monitoring (SRM) was employed to assess the ratio bewteen PsbO1 and PsbO2 in FL and MAL proteomes. Novel proteins, including a new PsbP domain-containing isoform, as well as several novel post-translational modifications and N-termini, are reported, and bi-dimensional separation of the lumen proteome identified several potential multi-protein oligomers in the thylakoid lumen.

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Formation of ER-lumenal intermediates during export of Plasmodium proteins containing transmembrane-like hydrophobic sequences

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2023-06-07 | PXD036788 | Pride

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