GreenCut protein CPLD 49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b 6 f complex accumulation
Abstract
Summary The GreenCut encompasses a suite of nucleus‐encoded proteins with orthologs among green lineage organisms (plants, green algae), but that are absent or poorly conserved in non‐photosynthetic/heterotrophic organisms. In Chlamydomonas reinhardtii , CPLD 49 ( C onserved in P lant L ineage and D iatoms 49 ) is an uncharacterized GreenCut protein that is critical for maintaining normal photosynthetic function. We demonstrate that a cpld49 mutant has impaired photoautotrophic growth under high‐light conditions. The mutant exhibits a nearly 90% reduction in the level of the cytochrome b 6 f complex (Cyt b 6 f ), which impacts linear and cyclic electron transport, but does not compromise the ability of the strain to perform state transitions. Furthermore, CPLD 49 strongly associates with thylakoid membranes where it may be part of a membrane protein complex with another GreenCut protein, CPLD 38; a mutant null for CPLD 38 also impacts Cyt b 6 f complex accumulation. We investigated several potential functions of CPLD 49, with some suggested by protein homology. Our findings are congruent with the hypothesis that CPLD 38 and CPLD 49 are part of a novel thylakoid membrane complex that primarily modulates accumulation, but also impacts the activity of the Cytmore »
- Authors:
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[1];
[2];
[2];
[3];
[1];
[5];
[6];
[7];
[8];
[9];
[10];
[6];
[2]
- Department of Biology Stanford University Stanford CA 94305 USA, Department of Plant Biology Carnegie Institution for Science Stanford CA 94305 USA
- Department of Plant Biology Carnegie Institution for Science Stanford CA 94305 USA
- Laboratoire de Bioénergétique et Biotechnologie des Bactéries et Microalgues CEA Cadarache Saint Paul lez Durance France
- Department of Biology Stanford University Stanford CA 94305 USA
- Department of Materials Science and Engineering Stanford University Stanford CA 94305 USA
- Department of Plant and Microbial Biology Howard Hughes Medical Institute University of California Berkeley CA 94720‐3102 USA, Molecular Biophysics and Integrated Bioimaging Division Lawrence Berkeley National Laboratory Berkeley CA 94720 USA
- Proteomics and Metabolomics Facility Colorado State University Fort Collins CO 80523 USA
- Department of Biology Colorado State University Fort Collins CO 80523 USA
- Institut für Molekulare Physiologie – Pflanzenbiochemie Johannes Gutenberg‐Universität 55099 Mainz Germany
- Institut de Biologie Physico‐Chimique CNRS‐UPMC Paris France
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1440805
- Grant/Contract Number:
- DE‐FG02‐07ER64427; DE‐FG02‐12ER16338
- Resource Type:
- Publisher's Accepted Manuscript
- Journal Name:
- The Plant Journal
- Additional Journal Information:
- Journal Name: The Plant Journal Journal Volume: 94 Journal Issue: 6; Journal ID: ISSN 0960-7412
- Publisher:
- Wiley-Blackwell
- Country of Publication:
- United Kingdom
- Language:
- English
Citation Formats
Wittkopp, Tyler M., Saroussi, Shai, Yang, Wenqiang, Johnson, Xenie, Kim, Rick G., Heinnickel, Mark L., Russell, James J., Phuthong, Witchukorn, Dent, Rachel M., Broeckling, Corey D., Peers, Graham, Lohr, Martin, Wollman, Francis‐André, Niyogi, Krishna K., and Grossman, Arthur R. GreenCut protein CPLD 49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b 6 f complex accumulation. United Kingdom: N. p., 2018.
Web. doi:10.1111/tpj.13915.
Wittkopp, Tyler M., Saroussi, Shai, Yang, Wenqiang, Johnson, Xenie, Kim, Rick G., Heinnickel, Mark L., Russell, James J., Phuthong, Witchukorn, Dent, Rachel M., Broeckling, Corey D., Peers, Graham, Lohr, Martin, Wollman, Francis‐André, Niyogi, Krishna K., & Grossman, Arthur R. GreenCut protein CPLD 49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b 6 f complex accumulation. United Kingdom. https://doi.org/10.1111/tpj.13915
Wittkopp, Tyler M., Saroussi, Shai, Yang, Wenqiang, Johnson, Xenie, Kim, Rick G., Heinnickel, Mark L., Russell, James J., Phuthong, Witchukorn, Dent, Rachel M., Broeckling, Corey D., Peers, Graham, Lohr, Martin, Wollman, Francis‐André, Niyogi, Krishna K., and Grossman, Arthur R. Wed .
"GreenCut protein CPLD 49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b 6 f complex accumulation". United Kingdom. https://doi.org/10.1111/tpj.13915.
@article{osti_1440805,
title = {GreenCut protein CPLD 49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b 6 f complex accumulation},
author = {Wittkopp, Tyler M. and Saroussi, Shai and Yang, Wenqiang and Johnson, Xenie and Kim, Rick G. and Heinnickel, Mark L. and Russell, James J. and Phuthong, Witchukorn and Dent, Rachel M. and Broeckling, Corey D. and Peers, Graham and Lohr, Martin and Wollman, Francis‐André and Niyogi, Krishna K. and Grossman, Arthur R.},
abstractNote = {Summary The GreenCut encompasses a suite of nucleus‐encoded proteins with orthologs among green lineage organisms (plants, green algae), but that are absent or poorly conserved in non‐photosynthetic/heterotrophic organisms. In Chlamydomonas reinhardtii , CPLD 49 ( C onserved in P lant L ineage and D iatoms 49 ) is an uncharacterized GreenCut protein that is critical for maintaining normal photosynthetic function. We demonstrate that a cpld49 mutant has impaired photoautotrophic growth under high‐light conditions. The mutant exhibits a nearly 90% reduction in the level of the cytochrome b 6 f complex (Cyt b 6 f ), which impacts linear and cyclic electron transport, but does not compromise the ability of the strain to perform state transitions. Furthermore, CPLD 49 strongly associates with thylakoid membranes where it may be part of a membrane protein complex with another GreenCut protein, CPLD 38; a mutant null for CPLD 38 also impacts Cyt b 6 f complex accumulation. We investigated several potential functions of CPLD 49, with some suggested by protein homology. Our findings are congruent with the hypothesis that CPLD 38 and CPLD 49 are part of a novel thylakoid membrane complex that primarily modulates accumulation, but also impacts the activity of the Cyt b 6 f complex. Based on motifs of CPLD 49 and the activities of other CPLD 49‐like proteins, we suggest a role for this putative dehydrogenase in the synthesis of a lipophilic thylakoid membrane molecule or cofactor that influences the assembly and activity of Cyt b 6 f .},
doi = {10.1111/tpj.13915},
journal = {The Plant Journal},
number = 6,
volume = 94,
place = {United Kingdom},
year = {Wed May 16 00:00:00 EDT 2018},
month = {Wed May 16 00:00:00 EDT 2018}
}
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