A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
The Thylakoid Membrane Proteome of Two Marine Diatoms Outlines Both Diatom-Specific and Species-Specific Features of the Photosynthetic Machinery
Tekijät: Grouneva I, Rokka A, Aro EM
Kustantaja: AMER CHEMICAL SOC
Julkaisuvuosi: 2011
Lehti: Journal of Proteome Research
Tietokannassa oleva lehden nimi: JOURNAL OF PROTEOME RESEARCH
Lehden akronyymi: J PROTEOME RES
Numero sarjassa: 12
Vuosikerta: 10
Numero: 12
Aloitussivu: 5338
Lopetussivu: 5353
Sivujen määrä: 16
ISSN: 1535-3893
DOI: https://doi.org/10.1021/pr200600f
Tiivistelmä
The thylakoid membrane of photoautotrophic organisms contains the main components of the photosynthetic electron transport chain. Detailed proteome maps of the thylakoid protein complexes of two marine diatoms, Thalassiosira pseudonana and Phaeodactylum tricornutum, were created by means of two-dimensional blue native (BN)/SDS-PAGE coupled with mass spectrometry analysis. One novel diatomspecific photosystem I (PS I)-associated protein was identified. A second plastid-targeted protein with possible PS I interaction was discovered to be restricted to the centric diatom species T. pseudonana. PGR5/PGRL homologues were found to be the only protein components of PS I-mediated cyclic electron transport common to both species. For the first time, evidence for a possible PSI localization of LI818-like light harvesting proteins (Lhcx) is presented. This study also advances the current knowledge on the light harvesting antenna composition and Lhcx expression in T. pseudonana on the protein level and presents details on the molecular distribution of Lhcx in diatoms. Above mentioned proteins and several others with unknown function provide a broad basis for further mutagenesis analysis, aiming toward further understanding of the composition and function of the photosynthetic apparatus of diatoms. The proteomics approach of this study further served as a tool to confirm and improve genome-derived protein models.
The thylakoid membrane of photoautotrophic organisms contains the main components of the photosynthetic electron transport chain. Detailed proteome maps of the thylakoid protein complexes of two marine diatoms, Thalassiosira pseudonana and Phaeodactylum tricornutum, were created by means of two-dimensional blue native (BN)/SDS-PAGE coupled with mass spectrometry analysis. One novel diatomspecific photosystem I (PS I)-associated protein was identified. A second plastid-targeted protein with possible PS I interaction was discovered to be restricted to the centric diatom species T. pseudonana. PGR5/PGRL homologues were found to be the only protein components of PS I-mediated cyclic electron transport common to both species. For the first time, evidence for a possible PSI localization of LI818-like light harvesting proteins (Lhcx) is presented. This study also advances the current knowledge on the light harvesting antenna composition and Lhcx expression in T. pseudonana on the protein level and presents details on the molecular distribution of Lhcx in diatoms. Above mentioned proteins and several others with unknown function provide a broad basis for further mutagenesis analysis, aiming toward further understanding of the composition and function of the photosynthetic apparatus of diatoms. The proteomics approach of this study further served as a tool to confirm and improve genome-derived protein models.
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