A screen for potential ferredoxin electron transfer partners uncovers new, redox dependent interactions

Autor(en): Hanke, G. T. 
Satomi, Y.
Shinmura, K.
Takao, T.
Hase, T.
Stichwörter: BIDIRECTIONAL HYDROGENASE; Biochemistry & Molecular Biology; Biophysics; CYANIDIUM-CALDARIUM; Electron transfer; Ferredoxin; GLNB GENE-PRODUCT; INORGANIC CARBON; NITROGEN ASSIMILATION; Photosynthesis; PHOTOSYSTEM-I; Redox regulation; RpaA; SHIKIMATE PATHWAY; SIGNAL-TRANSDUCTION PROTEINS; SOLUBLE HYDROGENASE; Synechocystis; TRANSFER COMPLEX
Erscheinungsdatum: 2011
Herausgeber: ELSEVIER SCIENCE BV
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volumen: 1814
Ausgabe: 2
Startseite: 366
Seitenende: 374
Zusammenfassung: 
Ferredoxin (Fd) is the primary soluble acceptor at the end of the photosynthetic electron transport chain, and is known to directly transfer electrons to a wide range of proteins for use in metabolism and regulatory processes. We have conducted a screen to identify new putative Fd interaction partners in the cyanobacteria Synechocystis sp. PCC 6803 using Fd-chromatography in combination with MALDI-TOF mass spectrometry. Many novel interactions were detected, including several redox enzymes, which are now candidates for further experiments to investigate electron transfer with Fd. In addition, some proteins with regulatory activity related to photosynthesis were identified. We cloned and expressed one such protein, known as RpaA, which is a specific regulator of energy transfer between phycobilisomes and PSI. Using the recombinant protein we confirmed direct interaction with Fd, and discovered that this was dependent on redox state. The screen for putative Fd-binding proteins was repeated, comparing oxidizing and reducing conditions, identifying many proteins whose interaction with Fd is redox dependent. These include several additional signaling molecules, among them the LexA repressor, Ycf53 and NIL which are all involved in interpreting the redox state of the cell. (C) 2010 Elsevier B.V. All rights reserved.
ISSN: 15709639
DOI: 10.1016/j.bbapap.2010.09.011

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