Abstract

Expression of Photosynthesis-Associated Nuclear Genes (PhANGs) is controlled by environmental stimuli and plastid-derived signals (“plastid signals”) transmitting the developmental and functional status of plastids to the nucleus. Arabidopsis genomes uncoupled (gun) mutants exhibit defects in plastid signaling, leading to ectopic expression of PhANGs in the absence of chloroplast development. GUN5 encodes the plastid-localized Mg-chelatase enzyme subunit (CHLH), and recent studies suggest that CHLH is a multifunctional protein involved in tetrapyrrole biosynthesis, plastid signaling and ABA responses in guard cells. To understand the basis of CHLH multifunctionality, we investigated 15 gun5 missense mutant alleles and transgenic lines expressing a series of truncated CHLH proteins in a severe gun5 allele (cch) background (tCHLHs, 10 different versions). Here, we show that Mg-chelatase function and plastid signaling are generally correlated; in contrast, based on the analysis of the gun5 missense mutant alleles, ABA-regulated stomatal control is distinct from these two other functions. We found that none of the tCHLHs could restore plastid-signaling or Mg-chelatase functions. Additionally, we found that both the C-terminal half and N-terminal half of CHLH function in ABA-induced stomatal movement.

Highlights

  • IntroductionCHLH ( called GENOMES UNCOUPLED 5, GUN5) is a multifunctional protein involved in chlorophyll biosynthesis, plastid-to-nucleus signaling, and abscisic acid (ABA) responses

  • CHLH is a multifunctional protein involved in chlorophyll biosynthesis, plastid-to-nucleus signaling, and abscisic acid (ABA) responses

  • CHLH is a plastidlocalized protein that has been studied as the largest (H) subunit of Mg-chelatase, which catalyzes the conversion of Protoporphyrin IX (Proto) to Mg-Protoporphyrin IX (MgProto), a key step in the tetrapyrrole biosynthesis pathway in plants (Tanaka et al, 2011)

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Summary

Introduction

CHLH ( called GENOMES UNCOUPLED 5, GUN5) is a multifunctional protein involved in chlorophyll biosynthesis, plastid-to-nucleus signaling, and ABA responses. The Arabidopsis mutants cch and gun− have respectively a Pro to Leu substitution at residue 642 (P642L) and an Ala to Val substitution at residue 990 (A990V). These positions map to P595 and A942 in the SynCHLH protein (Supplementary Figure 1), which are located respectively in domain III and at the junction between domains III and V (Chen et al, 2015). Because the cch and gun− mutant CHLH proteins can bind Proto but are catalytically inactive, it has been proposed that these mutations may introduce spatial hindrance and interfere with chelation (Davison and Hunter, 2011)

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