A1 Journal article – refereed

Two Proteins Homologous to PsbQ are Novel Subunits of the Chloroplast NAD(P)H Dehydrogenase




List of Authors: Suorsa M, Sirpio S, Paakkarinen V, Kumari N, Holmstrom M, Aro EM

Publisher: OXFORD UNIV PRESS

Publication year: 2010

Journal: Plant and Cell Physiology

Journal name in source: PLANT AND CELL PHYSIOLOGY

Journal acronym: PLANT CELL PHYSIOL

Volume number: 51

Issue number: 6

Number of pages: 7

ISSN: 0032-0781

DOI: http://dx.doi.org/10.1093/pcp/pcq070


Abstract
The PsbQ-like (PQL) proteins 1 and 2, previously shown to be located in the thylakoid lumen of Arabidopsis thaliana, are homologous to PSII oxygen-evolving complex protein PsbQ. Nevertheless, pql mutants showed no defects in PSII but instead the activity of the chloroplast NAD(P)H dehydrogenease (NDH) complex was severely impaired. In line with this observation, the NDH subunits were low in abundance in pql mutants, and, conversely, ndh mutants strongly down-regulated the accumulation of the PQL proteins. In addition, the PQL2 protein was up-regulated in mutant plants deficient in the PSI complex or the thylakoid membrane-bound ferredoxin-NADP+ oxidoreductase, whereas in pql mutants the PSI complex was slightly up-regulated. Taken together, the two PQL proteins are shown to be novel subunits of the lumenal protuberance of the NDH complex.


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