Literature DB >> 21376623

Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex.

Kentaro Ifuku1, Kunio Ido, Fumihiko Sato.   

Abstract

The PsbP and PsbQ proteins are extrinsic subunits of the photosystem II (PSII) supercomplex, which are found in green plants including higher plants and green algae. These proteins are thought to have evolved from their cyanobacterial homologs; cyanoP and cyanoQ respectively. It has been suggested that the functions of PsbP and PsbQ have largely changed from those of cyanoP and cyanoQ. In addition, multiple isoforms and homologs of PsbP and PsbQ were found in green plants, indicating that the acquisition of PsbP and PsbQ in PSII is not a direct path but a result of intensive functional divergence during evolution from cyanobacterial endosymbiont to chloroplast. In this review, we highlight newly introduced topics related to the functions and structures of both PsbP and PsbQ proteins. The present data suggest that PsbP together with PsbQ have specific and important roles in coordinating the activity of the donor and acceptor sides of PSII and stabilizing the active form of the PSII-light-harvesting complex II (LHCII) supercomplex.
Copyright © 2011 Elsevier B.V. All rights reserved.

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Year:  2011        PMID: 21376623     DOI: 10.1016/j.jphotobiol.2011.02.006

Source DB:  PubMed          Journal:  J Photochem Photobiol B        ISSN: 1011-1344            Impact factor:   6.252


  22 in total

1.  The conserved His-144 in the PsbP protein is important for the interaction between the PsbP N-terminus and the Cyt b559 subunit of photosystem II.

Authors:  Kunio Ido; Shusuke Kakiuchi; Chihiro Uno; Taishi Nishimura; Yoichiro Fukao; Takumi Noguchi; Fumihiko Sato; Kentaro Ifuku
Journal:  J Biol Chem       Date:  2012-06-15       Impact factor: 5.157

2.  Structural changes of the oxygen-evolving complex in photosystem II during the catalytic cycle.

Authors:  Carina Glöckner; Jan Kern; Matthias Broser; Athina Zouni; Vittal Yachandra; Junko Yano
Journal:  J Biol Chem       Date:  2013-06-13       Impact factor: 5.157

3.  Characterization of a Synechocystis sp. PCC 6803 double mutant lacking the CyanoP and Ycf48 proteins of Photosystem II.

Authors:  Simon A Jackson; Julian J Eaton-Rye
Journal:  Photosynth Res       Date:  2015-03-24       Impact factor: 3.573

4.  Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts.

Authors:  Debjani Pal; Kristen Fite; Carole Dabney-Smith
Journal:  Plant Physiol       Date:  2012-12-03       Impact factor: 8.340

Review 5.  The PsbP family of proteins.

Authors:  Terry M Bricker; Johnna L Roose; Pengpeng Zhang; Laurie K Frankel
Journal:  Photosynth Res       Date:  2013-04-07       Impact factor: 3.573

6.  In vivo system for analyzing the function of the PsbP protein using Chlamydomonas reinhardtii.

Authors:  Taishi Nishimura; Fumihiko Sato; Kentaro Ifuku
Journal:  Photosynth Res       Date:  2017-03-24       Impact factor: 3.573

7.  Determination of chemical identity and occupancy from experimental density maps.

Authors:  Jimin Wang
Journal:  Protein Sci       Date:  2017-11-02       Impact factor: 6.725

Review 8.  Structural, functional and auxiliary proteins of photosystem II.

Authors:  Cristina Pagliano; Guido Saracco; James Barber
Journal:  Photosynth Res       Date:  2013-02-17       Impact factor: 3.573

9.  PHOTOSYSTEM II SUBUNIT R is required for efficient binding of LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 to photosystem II-light-harvesting supercomplexes in Chlamydomonas reinhardtii.

Authors:  Huidan Xue; Ryutaro Tokutsu; Sonja Verena Bergner; Martin Scholz; Jun Minagawa; Michael Hippler
Journal:  Plant Physiol       Date:  2015-02-19       Impact factor: 8.340

10.  Cross-linking evidence for multiple interactions of the PsbP and PsbQ proteins in a higher plant photosystem II supercomplex.

Authors:  Kunio Ido; Jon Nield; Yoichiro Fukao; Taishi Nishimura; Fumihiko Sato; Kentaro Ifuku
Journal:  J Biol Chem       Date:  2014-06-09       Impact factor: 5.157

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