Journal Article

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

Marjaana Suorsa, Sari Sirpiö, Virpi Paakkarinen, Nilima Kumari, Maija Holmström and Eva-Mari Aro

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 51, issue 6, pages 877-883
Published in print June 2010 | ISSN: 0032-0781
Published online May 2010 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcq070
Two Proteins Homologous to PsbQ are Novel Subunits of the Chloroplast NAD(P)H Dehydrogenase

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  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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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.

Keywords: Arabidopsis; Chloroplast; Cyclic electron transfer; Lumen; NAD(P)H dehydrogenase complex; Thylakoid

Journal Article.  4065 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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