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Translation and Co-Translational Membrane Engagement of Plastid-Encoded Chlorophyll-Binding Proteins are not Influenced by Chlorophyll Availability in Maize

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Zoschke,  R.
Translational Regulation in Plants, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Zoschke, R., Chotewutmontri, P., & Barkan, A. (2017). Translation and Co-Translational Membrane Engagement of Plastid-Encoded Chlorophyll-Binding Proteins are not Influenced by Chlorophyll Availability in Maize. Frontiers in Plant Science, 8: 385. doi:10.3389/fpls.2017.00385.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-DC7A-A
Abstract
Chlorophyll is an indispensable constituent of the photosynthetic machinery in green organisms. Bound by apoproteins of photosystems I and II, chlorophyll performs light-harvesting and charge separation. Due to the phototoxic nature of free chlorophyll and its precursors, chlorophyll synthesis is regulated to comply with the availability of nascent chlorophyll-binding apoproteins. Conversely, the synthesis and co-translational insertion of such proteins into the thylakoid membrane have been suggested to be influenced by chlorophyll availability. In this study, we addressed these hypotheses by using ribosome profiling to examine the synthesis and membrane targeting of chlorophyll-binding apoproteins in chlorophyll-deficient chlH maize mutants (Zm-chlH). ChlH encodes the H subunit of the magnesium chelatase (also known as GUN5), which catalyzes the first committed step in chlorophyll synthesis. Our results show that the number and distribution of ribosomes on plastid mRNAs encoding chlorophyll-binding apoproteins are not substantially altered in Zm-chlH mutants, suggesting that chlorophyll has no impact on ribosome dynamics. Additionally, a Zm-chlH mutation does not change the amino acid position at which nascent chlorophyll-binding apoproteins engage the thylakoid membrane, nor the efficiency with which membrane-engagement occurs. Together, these results provide evidence that chlorophyll availability does not selectively activate the translation of plastid mRNAs encoding chlorophyll apoproteins. Our results imply that co- or post-translational proteolysis of apoproteins is the primary mechanism that adjusts apoprotein abundance to chlorophyll availability in plants.