Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Chemical Protein Crosslinking-Coupled Mass Spectrometry Reveals Interaction of LHCI with LHCII and LHCSR3 in C. reinhardtii

Laura Mosebach
,
Shin-Ichiro Ozawa
ORCID logo ,
Muhammad Younas
,
Huidan Xue
,
Martin Scholz
,
Yuichiro Takahashi
,
MIchael Hippler
* ORCID logo
Version 1 : Received: 15 April 2024 / Approved: 16 April 2024 / Online: 16 April 2024 (15:57:00 CEST)

How to cite: Mosebach, L.; Ozawa, S.; Younas, M.; Xue, H.; Scholz, M.; Takahashi, Y.; Hippler, M. Chemical Protein Crosslinking-Coupled Mass Spectrometry Reveals Interaction of LHCI with LHCII and LHCSR3 in C. reinhardtii. Preprints 2024, 2024041057. https://doi.org/10.20944/preprints202404.1057.v1 Mosebach, L.; Ozawa, S.; Younas, M.; Xue, H.; Scholz, M.; Takahashi, Y.; Hippler, M. Chemical Protein Crosslinking-Coupled Mass Spectrometry Reveals Interaction of LHCI with LHCII and LHCSR3 in C. reinhardtii. Preprints 2024, 2024041057. https://doi.org/10.20944/preprints202404.1057.v1

Abstract

The photosystem I (PSI) of the green alga Chlamydomonas reinhardtii associates with 10 light-harvesting proteins (LHCI) to form the PSI-LHCI complex. Binding of LHCII to PSI may also occur and is controlled by a process called state transitions. Hereby, two LHCII trimers bind to the PSAL, PSAH and PSAO side of PSI to produce the PSI-LHCI-LHCII complex. In this work, we took advantage of chemical crosslinking of proteins in conjunction with mass spectrometry to identify protein-protein interactions between the light-harvesting proteins of PSI and PSII. We detected binding of LHCBM proteins to the LHCA1-PSAG side of PSI and identified protein-protein interactions of LHCSR3 with LHCA5 and LHCA3. Our data indicate that the binding of LHCII to PSI is more versatile as anticipated and reveal that LHCSR3 likely regulates excitation energy transfer to the PSI core via LHCA5/LHCA3.

Keywords

photosystem I; chemical crosslinking; mass spectrometry; Chlamydomonas reinhardtii

Subject

Biology and Life Sciences, Plant Sciences

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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