A1 Refereed original research article in a scientific journal

TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle




AuthorsSirpio S, Allahverdiyeva Y, Suorsa M, Paakkarinen V, Vainonen J, Battchikova N, Aro EM

PublisherPORTLAND PRESS LTD

Publication year2007

Journal:Biochemical Journal

Journal name in sourceBIOCHEMICAL JOURNAL

Journal acronymBIOCHEM J

Volume406

First page 415

Last page425

Number of pages11

ISSN0264-6021

DOIhttps://doi.org/10.1042/BJ20070460


Abstract
A proteome analysis of Arabidopsis thaliana thylakoid-associated polysome nascent chain complexes was performed to find novel proteins involved in the biogenesis, maintenance and turnover of thylakoid protein complexes, in particular the PSII (photosystem II) complex, which exhibits a high turnover rate. Four unknown proteins were identified, of which TLP18.3 ((t) under bar hylakoid (l) under bar umen (p) under bar rotein of 18.3 kDa) was selected for further analysis. The Arabidopsis mutants (SALK_109618 and GABI-Kat 459D12) lacking the TLP18.3 protein showed higher susceptibility of PSII to photoinhibition. The increased susceptibility of Delta TLP18.3 plants to high light probably originates from an inefficient reassembly of PSII monomers into dimers in the grana stacks, as well as from an impaired turnover of the D1 protein in stroma exposed thylakoids. Such dual function of the TLP18.3 protein is in accordance with its even distribution between the grana and stroma thylakoids. Notably, the lack of the TLP18.3 protein does not lead to a severe collapse of the PSII complexes, suggesting a redundancy of proteins assisting these particular repair steps to assure functional PSII. The Delta TLP18.3 plants showed no clear visual phenotype under standard growth conditions, but when challenged by fluctuating light during growth, the retarded growth of Delta TLP18.3 plants was evident.



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