Vertaisarvioitu alkuperäisartikkeli tai data-artikkeli tieteellisessä aikakauslehdessä (A1)
Characterization of the Free and Membrane-Associated Fractions of the Thylakoid Lumen Proteome in Arabidopsis thaliana
Julkaisun tekijät: Gollan Peter J., Trotta Andrea, Bajwa Azfar A., Mancini Ilaria, Aro Eva-Mari
Kustantaja: MDPI
Julkaisuvuosi: 2021
Journal: International Journal of Molecular Sciences
Tietokannassa oleva lehden nimi: International journal of molecular sciences
Lehden akronyymi: Int J Mol Sci
Volyymi: 22
Julkaisunumero: 15
ISSN: 1422-0067
eISSN: 1422-0067
DOI: http://dx.doi.org/10.3390/ijms22158126
Rinnakkaistallenteen osoite: https://research.utu.fi/converis/portal/detail/Publication/66958346
The thylakoid lumen 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 analyze the contents of each proteome. These results identified 60 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 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 protein oligomers in the thylakoid lumen.
Ladattava julkaisu This is an electronic reprint of the original article. |  |
