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Proteome map of the chloroplast lumen of Arabidopsis thaliana
Södertörn University, Avdelning Naturvetenskap. Karolinska Institute.
Södertörn University, Avdelning Naturvetenskap. Stockholm University.
Institute for Genomic Research, Rockville, USA.
Stockholm University.
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2002 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, no 10, 8354-8365 p.Article in journal (Refereed) Published
Abstract [en]

The thylakoid membrane of the chloroplast is the center of oxygenic photosynthesis. To better understand the function of the luminal compartment within the thylakoid network, we have carried out a systematic characterization of the luminal thylakoid proteins from the model organism Arabidopsis thaliana. Our data show that the thylakoid lumen has its own specific proteome, of which 36 proteins were identified. Besides a large group of peptidyl-prolyl cis-trans isomerases and pro. teases, a family of novel PsbP domain proteins was found. An analysis of the luminal signal peptides showed that 19 of 36 luminal precursors were marked by a twin-arginine motif for import via the Tat pathway. To compare the model organism Arabidopsis with another typical higher plant, we investigated the proteome from the thylakoid lumen of spinach and found that the luminal proteins from both plants corresponded well. As a complement to our experimental investigation, we made a theoretical prediction of the luminal proteins from the whole Arabidopsis genome and estimated that the thylakoid lumen of the chloroplast contains similar to80 proteins.

Place, publisher, year, edition, pages
2002. Vol. 277, no 10, 8354-8365 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:sh:diva-15812DOI: 10.1074/jbc.M108575200ISI: 000174268000094PubMedID: 11719511ScopusID: 2-s2.0-0037040944OAI: oai:DiVA.org:sh-15812DiVA: diva2:508477
Available from: 2012-03-08 Created: 2012-03-07 Last updated: 2017-02-08Bibliographically approved
In thesis
1. Overview and characterisation of the thylakoid lumen of higher plants
Open this publication in new window or tab >>Overview and characterisation of the thylakoid lumen of higher plants
2006 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In higher plants, chloroplasts are the site for the photosynthetic reactions, converting solar energy to chemical energy. Within the chloroplast the thylakoid membrane network encloses the soluble lumen compartment. Until recently the knowledge of the lumen composition and function was limited, but a more profound understanding of the thylakoid lumen content is gradually emerging. The discovery that the thylakoid lumen contains numerous enzymes, besides the already known proteins directly involved or associated with the photosynthetic reactions, have changed the view on this compartment.

The first part of the thesis the lumen proteome maps of Arabidopsis and spinach were resolved. These two proteome maps showed good correlation and the same protein groups were represented in the two proteomes. Thirty eight proteins were identified and in combination with an in silico prediction for the proteome it was estimated that at least 80 different proteins are lumen located.

The second part was to further investigate the functions of two lumen localized proteins, the cyclophilin AtCYP20-2 and peroxiredoxin Q (PrxQ). AtCYP20-2 is suggested to be responsible for the major peptidyl prolyl cis/trans isomerases (PPIase) activity in the lumen. In AtCYP20-2 knockout mutants the total PPIase activity is not altered, instead AtFKBP13 may be oxidatively activated to compensate for the loss of AtCYP20-2. With respect to the PrxQ protein we were able to show that it is a lumenal protein that seems to exist as a soluble pool in the lumen as no interaction with the thylakoid membrane could be detected.

In the last part of this thesis the dynamics of the thylakoid membrane and lumen proteome were studied during oxidative stress. Important changes to the proteome were observed in response to the stress treatment, including abundance changes of proteins related to photosynthesis, as well as proteins not previously identified in relation to stress.

Place, publisher, year, edition, pages
Stockholm: Stockholm University, 2006. 51 p.
Keyword
Arablidopsis, thylakoid lumen, AtCYP20-2, Peroxiredoxin Q, oxidative stress
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:sh:diva-31471 (URN)91-7155-299-5 (ISBN)
Public defence
2006-11-24, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, 10:00
Opponent
Supervisors
Available from: 2016-12-20 Created: 2016-12-20 Last updated: 2016-12-20Bibliographically approved
2. The chloroplast lumen proteome of Arabidopsis thaliana
Open this publication in new window or tab >>The chloroplast lumen proteome of Arabidopsis thaliana
2006 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In plants, the chloroplast organelles host the photosynthetic machinery, which catalyzes the conversion of light energy to chemical energy used for synthesis of carbohydrates. Inside the chloroplast, the lumen compartment forms an integral part of the thylakoid network that performs the light reactions of photosynthesis. Despite intensive research within the field of photosynthesis, the lumen located proteins were relatively unexplored. To get insight into the lumen proteins and their roles in photosynthesis this thesis aimed at characterising the chloroplast lumen proteome. A 2-dimensional protein map of the lumen proteome of Arabidopsis thaliana revealed a high protein content within this chloroplast compartment. Thirty-eight proteins were experimentally identified demonstrating that the chloroplast lumen contains it own specific proteome. Comparison of the Arabidopsis chloroplast lumen proteome with the spinach lumen proteome showed good correlation and demonstrated that Arabidopsis can serve as a model for characterising the lumen proteins. An in silico determination of the chloroplast lumen proteome from the Arabidopsis genome sequence data showed that the experimentally identified proteins are good representatives of the proteome. Combining the in silico proteome with the experimental proteome, the chloroplast lumen estimates to contain at least 80 different proteins. The putative ascorbate peroxidase TL29 detected in the thylakoid lumen was biochemically characterised. The protein associated to the PSII-enriched grana membrane fraction by electrostatic forces and accumulated upon high light illumination. Functional analysis showed that the TL29 protein is not a peroxidase but was able to bind ascorbate and may be involved in regulating the ascorbate levels in the chloroplast lumen. The dynamics of the lumen proteome were studied during the cold acclimation process. The lumen proteome was relatively insensitive to cold stress but important changes to the proteome were observed in the long-term developmental response to cold. These included changes in abundance of the different isoforms of the extrinsic PSII subunits, the PSII assembly factor Hcf136 and immunophilins. In comparison, the stroma proteome responded at an earlier stage in the acclimation process. Changes to the stroma proteome involved proteins related to photosynthesis, other plastid metabolism, hormone biosynthesis, and stress & signal transduction.

Place, publisher, year, edition, pages
Stockholm: Karolinska instiutet, 2006. 55 p.
National Category
Biological Sciences
Identifiers
urn:nbn:se:sh:diva-31996 (URN)91-7140-654-9 (ISBN)
Public defence
2006-05-24, MA648, Alfred Nobels allé 7, Huddinge, 10:00 (English)
Opponent
Supervisors
Available from: 2017-02-08 Created: 2017-02-08 Last updated: 2017-02-08Bibliographically approved

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