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Front Plant Sci. 2017 Mar 28;8:385. doi: 10.3389/fpls.2017.00385. eCollection 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

Reimo Zoschke, Prakitchai Chotewutmontri, Alice Barkan

Affiliations

  1. Max Planck Institute of Molecular Plant Physiology Potsdam, Germany.
  2. Institute of Molecular Biology, University of Oregon, Eugene OR, USA.

PMID: 28400776 PMCID: PMC5368244 DOI: 10.3389/fpls.2017.00385

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

Keywords: ChlH; GUN5; chlorophyll; chloroplast; maize; ribosome profiling; translation

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