Journal Browser

► Journal Browser

Special Issue Editor

Prof. Dr. Wolfgang P. Schröder

E-Mail Website
Guest Editor

Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden
Interests: photosynthesis; chloroplast; thylakoid structure and function

Special Issue Information

Dear Colleagues,

The chloroplast is the photosynthetic organelle of green algae and higher plants. The chloroplast architecture comprises an envelope membrane, which encloses the soluble stroma as well as the highly specialized thylakoid membrane. The stromal compartment contains mainly the components of the Calvin cycle, which are required for the fixation of carbon dioxide. The thylakoids, on the other hand, carry out the light reactions of photosynthesis, leading to the production of NADPH and ATP and as a byproduct the oxygen that we breathe. The thylakoid membrane has a characteristic flat shape and is differentiated into appressed grana stacks and single non-appressed stroma-exposed lamellae. The inner surface of the thylakoid membrane encloses a narrow, continuous compartment—the lumen.

The thylakoid lumen is known to be important for the formation of a proton gradient over the thylakoid membrane, which is needed for ATP synthesis; supporting and stabilizing oxygen evolution; and linking the electron transport between Photosystems II and I. It is now more than 20 years since the first pioneering proteomic analysis of the lumen compartment was published. This study showed that the lumen compartment contains a specific proteome with more than 40 unique proteins from various protein classes and several with unknown function. This has opened a new research avenue with many exciting new aspects, and it has become clear that the lumen-located proteins play a crucial role in numerous processes, most often linked with regulating thylakoid biogenesis and the activity and turnover of photosynthetic protein complexes. This emphasizes the important role of the thylakoid lumen for photosynthetic electron transfer and ultimately for plant fitness.

Prof. Dr. Wolfgang P. Schröder
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

higher plant
photosynthesis
light stress
structure of thylakoids
lumen
protein import
pH gradient
protein interaction
lipids
chaperones

Published Papers (2 papers)

Download All Papers

Research

Jump to: Review

21 pages, 16558 KiB

Open AccessFeature PaperArticle

Characterization of the Free and Membrane-Associated Fractions of the Thylakoid Lumen Proteome in Arabidopsis thaliana

by Peter J. Gollan, Andrea Trotta, Azfar A. Bajwa, Ilaria Mancini and Eva-Mari Aro

Int. J. Mol. Sci. 2021, 22(15), 8126; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22158126 - 29 Jul 2021

Cited by 5 | Viewed by 3021

Abstract

The thylakoid lumen houses proteins that are vital for photosynthetic electron transport, including water-splitting at photosystem (PS) II and shuttling of electrons from cytochrome b₆f to PSI. Other lumen proteins maintain photosynthetic activity through biogenesis and turnover of PSII complexes. Although all lumen proteins are soluble, these known details have highlighted interactions of some lumen proteins with thylakoid membranes or thylakoid-intrinsic proteins. Meanwhile, the functional details of most lumen proteins, as well as their distribution between the soluble and membrane-associated lumen fractions, remain unknown. The current study isolated the soluble free lumen (FL) and membrane-associated lumen (MAL) fractions from Arabidopsis thaliana, and used gel- and mass spectrometry-based proteomics methods to analyze the contents of each proteome. These results identified 60 lumenal proteins, and clearly distinguished the difference between the FL and MAL proteomes. The most abundant proteins in the FL fraction were involved in PSII assembly and repair, while the MAL proteome was enriched in proteins that support the oxygen-evolving complex (OEC). Novel proteins, including a new PsbP domain-containing isoform, as well as several novel post-translational modifications and N-termini, are reported, and bi-dimensional separation of the lumen proteome identified several protein oligomers in the thylakoid lumen. Full article

(This article belongs to the Special Issue Advances in Our Understanding of the Plant Thylakoid and Its Lumen—from Empty Space to Crowded Compartment)

► Show Figures

Figure 1

Review

Jump to: Research

21 pages, 1975 KiB

Open AccessReview

Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen

by Noritoshi Inagaki

Int. J. Mol. Sci. 2022, 23(5), 2520; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23052520 - 25 Feb 2022

Cited by 9 | Viewed by 2869

Abstract

In oxygenic photosynthetic organisms, D1 protein, a core subunit of photosystem II (PSII), displays a rapid turnover in the light, in which D1 proteins are distinctively damaged and immediately removed from the PSII. In parallel, as a repair process, D1 proteins are synthesized and simultaneously assembled into the PSII. On this flow, the D1 protein is synthesized as a precursor with a carboxyl-terminal extension, and the D1 processing is defined as a step for proteolytic removal of the extension by a specific protease, CtpA. The D1 processing plays a crucial role in appearance of water-oxidizing capacity of PSII, because the main chain carboxyl group at carboxyl-terminus of the D1 protein, exposed by the D1 processing, ligates a manganese and a calcium atom in the Mn₄CaO₅-cluster, a special equipment for water-oxidizing chemistry of PSII. This review focuses on the D1 processing and discusses it from four angles: (i) Discovery of the D1 processing and recognition of its importance: (ii) Enzyme involved in the D1 processing: (iii) Efforts for understanding significance of the D1 processing: (iv) Remaining mysteries in the D1 processing. Through the review, I summarize the current status of our knowledge on and around the D1 processing. Full article

(This article belongs to the Special Issue Advances in Our Understanding of the Plant Thylakoid and Its Lumen—from Empty Space to Crowded Compartment)

► Show Figures