D1 fragmentation in photosystem II repair caused by photo-damage of a two-step model

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Light energy drives photosynthesis, but it simultaneously inactivates photosynthetic mechanisms. A major target site of photo-damage is photosystem II (PSII). It further targets one reaction center protein, D1, which is maintained efficiently by the PSII repair cycle. Two proteases, FtsH and Deg, are known to contribute to this process, respectively, by efficient degradation of photo-damaged D1 protein processively and endoproteolytically. This study tested whether the D1 cleavage accomplished by these proteases is affected by different monochromic lights such as blue and red light-emitting-diode light sources, remaining mindful that the use of these lights distinguishes the current models for photoinhibition: the excess-energy model and the two-step model. It is noteworthy that in the two-step model, primary damage results from the absorption of light energy in the Mn-cluster, which can be enhanced by a blue rather than a red light source. Results showed that blue and red lights affect D1 degradation differently. One prominent finding was that D1 fragmentation that is specifically generated by luminal Deg proteases was enhanced by blue light but not by red light in the mutant lacking FtsH2. Although circumstantial, this evidence supports a two-step model of PSII photo-damage. We infer that enhanced D1 fragmentation by luminal Deg proteases is a response to primary damage at the Mn-cluster.

Original languageEnglish
Pages (from-to)409-416
Number of pages8
JournalPhotosynthesis Research
Volume126
Issue number2-3
DOIs
Publication statusPublished - Apr 19 2015

Fingerprint

Photosystem II Protein Complex
photosystem II
red light
Repair
Light
proteinases
blue light
D1 protein
Peptide Hydrolases
energy
Light sources
degradation
photoinhibition
Degradation
Photosynthesis
photosynthesis
Light emitting diodes
mutants
Proteins

Keywords

  • Chloroplast protease
  • D1 degradation
  • Deg
  • FtsH
  • Photoinhibition
  • PSII repair

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology
  • Biochemistry

Cite this

@article{bd01094091444adba933ea368f9dbe8b,
title = "D1 fragmentation in photosystem II repair caused by photo-damage of a two-step model",
abstract = "Light energy drives photosynthesis, but it simultaneously inactivates photosynthetic mechanisms. A major target site of photo-damage is photosystem II (PSII). It further targets one reaction center protein, D1, which is maintained efficiently by the PSII repair cycle. Two proteases, FtsH and Deg, are known to contribute to this process, respectively, by efficient degradation of photo-damaged D1 protein processively and endoproteolytically. This study tested whether the D1 cleavage accomplished by these proteases is affected by different monochromic lights such as blue and red light-emitting-diode light sources, remaining mindful that the use of these lights distinguishes the current models for photoinhibition: the excess-energy model and the two-step model. It is noteworthy that in the two-step model, primary damage results from the absorption of light energy in the Mn-cluster, which can be enhanced by a blue rather than a red light source. Results showed that blue and red lights affect D1 degradation differently. One prominent finding was that D1 fragmentation that is specifically generated by luminal Deg proteases was enhanced by blue light but not by red light in the mutant lacking FtsH2. Although circumstantial, this evidence supports a two-step model of PSII photo-damage. We infer that enhanced D1 fragmentation by luminal Deg proteases is a response to primary damage at the Mn-cluster.",
keywords = "Chloroplast protease, D1 degradation, Deg, FtsH, Photoinhibition, PSII repair",
author = "Yusuke Kato and Shinichiro Ozawa and Yuichiro Takahashi and Wataru Sakamoto",
year = "2015",
month = "4",
day = "19",
doi = "10.1007/s11120-015-0144-7",
language = "English",
volume = "126",
pages = "409--416",
journal = "Photosynthesis Research",
issn = "0166-8595",
publisher = "Springer Netherlands",
number = "2-3",

}

TY - JOUR

T1 - D1 fragmentation in photosystem II repair caused by photo-damage of a two-step model

AU - Kato, Yusuke

AU - Ozawa, Shinichiro

AU - Takahashi, Yuichiro

AU - Sakamoto, Wataru

PY - 2015/4/19

Y1 - 2015/4/19

N2 - Light energy drives photosynthesis, but it simultaneously inactivates photosynthetic mechanisms. A major target site of photo-damage is photosystem II (PSII). It further targets one reaction center protein, D1, which is maintained efficiently by the PSII repair cycle. Two proteases, FtsH and Deg, are known to contribute to this process, respectively, by efficient degradation of photo-damaged D1 protein processively and endoproteolytically. This study tested whether the D1 cleavage accomplished by these proteases is affected by different monochromic lights such as blue and red light-emitting-diode light sources, remaining mindful that the use of these lights distinguishes the current models for photoinhibition: the excess-energy model and the two-step model. It is noteworthy that in the two-step model, primary damage results from the absorption of light energy in the Mn-cluster, which can be enhanced by a blue rather than a red light source. Results showed that blue and red lights affect D1 degradation differently. One prominent finding was that D1 fragmentation that is specifically generated by luminal Deg proteases was enhanced by blue light but not by red light in the mutant lacking FtsH2. Although circumstantial, this evidence supports a two-step model of PSII photo-damage. We infer that enhanced D1 fragmentation by luminal Deg proteases is a response to primary damage at the Mn-cluster.

AB - Light energy drives photosynthesis, but it simultaneously inactivates photosynthetic mechanisms. A major target site of photo-damage is photosystem II (PSII). It further targets one reaction center protein, D1, which is maintained efficiently by the PSII repair cycle. Two proteases, FtsH and Deg, are known to contribute to this process, respectively, by efficient degradation of photo-damaged D1 protein processively and endoproteolytically. This study tested whether the D1 cleavage accomplished by these proteases is affected by different monochromic lights such as blue and red light-emitting-diode light sources, remaining mindful that the use of these lights distinguishes the current models for photoinhibition: the excess-energy model and the two-step model. It is noteworthy that in the two-step model, primary damage results from the absorption of light energy in the Mn-cluster, which can be enhanced by a blue rather than a red light source. Results showed that blue and red lights affect D1 degradation differently. One prominent finding was that D1 fragmentation that is specifically generated by luminal Deg proteases was enhanced by blue light but not by red light in the mutant lacking FtsH2. Although circumstantial, this evidence supports a two-step model of PSII photo-damage. We infer that enhanced D1 fragmentation by luminal Deg proteases is a response to primary damage at the Mn-cluster.

KW - Chloroplast protease

KW - D1 degradation

KW - Deg

KW - FtsH

KW - Photoinhibition

KW - PSII repair

UR - http://www.scopus.com/inward/record.url?scp=84942831547&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84942831547&partnerID=8YFLogxK

U2 - 10.1007/s11120-015-0144-7

DO - 10.1007/s11120-015-0144-7

M3 - Article

C2 - 25893898

AN - SCOPUS:84942831547

VL - 126

SP - 409

EP - 416

JO - Photosynthesis Research

JF - Photosynthesis Research

SN - 0166-8595

IS - 2-3

ER -