Posttranslational control of tetrapyrrole biosynthesis: Interacting proteins, chaperones, auxiliary factors

Herbst, Josephine; Hey, D.; Grimm, Bernhard

doi:10.1016/bs.abr.2019.01.001

Cited by 6 publications

(7 citation statements)

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“…The formation of MgP by MgCh is a key step in Chl biosynthesis, and the strict control of MgCh activity facilitates an efficient supply of Chl (Tanaka et al ., 2011; Herbst et al ., 2019). We found that MORF2 interacts with GUN4 and three subunits of the MgCh enzyme complex (CHLD, CHLI1 and CHLH) in N. benthamiana leaves (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Tetrapyrrole biosynthesis is tightly controlled to ensure the adequate supply of tetrapyrrole end products for plant growth and to avoid the accumulation of photoreactive tetrapyrrole intermediates, which could trigger photooxidative damage (Jung et al ., 2008). At the post‐translational level, molecular chaperones, auxiliary factors and interacting proteins cooperate to regulate the activity, stability and sub‐chloroplast localization as well as complex formation of the TBS enzymes (Herbst et al ., 2019). For example, the stability and structural integrity of the initial ALA‐synthesizing enzyme, glutamyl‐tRNA reductase (GluTR), is maintained by means of GluTR‐binding protein (GBP) and the chloroplast signal recognition particle 43 (cpSRP43), respectively.…”

Section: Introductionmentioning

confidence: 99%

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Two chloroplast‐localized MORF proteins act as chaperones to maintain tetrapyrrole biosynthesis

Yuan

et al. 2022

New Phytologist

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Tetrapyrroles have essential functions as pigments and cofactors during plant growth and development, and the tetrapyrrole biosynthesis pathway is tightly controlled. Multiple organellar RNA editing factors (MORFs) are required for editing of a wide variety of RNA sites in chloroplasts and mitochondria, but their biochemical properties remain elusive.Here, we uncovered the roles of chloroplast-localized MORF2 and MORF9 in modulating tetrapyrrole biosynthesis and embryogenesis in Arabidopsis thaliana. The lack or reduced transcripts of MORF2 or MORF9 significantly affected biosynthesis of the tetrapyrrole precursor 5-aminolevulinic acid and accumulation of Chl and other tetrapyrrole intermediates.MORF2 directly interacts with multiple tetrapyrrole biosynthesis enzymes and regulators, including NADPH:PROTOCHLOROPHYLLIDE OXIDOREDUCTASE B (PORB) and GENOMES UNCOUPLED4 (GUN4). Strikingly, MORF2 and MORF9 display holdase chaperone activity, alleviate the aggregation of PORB in vitro, and are essential for POR accumulation in vivo. Moreover, both MORF2 and MORF9 significantly stimulate magnesium chelatase activity.Our findings reveal a previously unknown biochemical property of MORF proteins as chaperones and point to a new layer of post-translational control of the tightly regulated tetrapyrrole biosynthesis in plants.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Two chloroplast‐localized MORF proteins act as chaperones to maintain tetrapyrrole biosynthesis

Yuan

et al. 2022

New Phytologist

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“…Again, all the predictions placed both CPOX to the plastid ( Figure 2 ). PPOX and FECH were found to form a complex allowing efficient channeling of metabolites through the thylakoid membranes, which protects the highly reactive protoporphyrinogen IX [ 73 , 74 ]. Therefore, these enzymes should share the same compartment.…”

Section: Discussionmentioning

confidence: 99%

Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia

Richtová

Sheiner

Gruber

et al. 2021

IJMS

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Heme biosynthesis is essential for almost all living organisms. Despite its conserved function, the pathway’s enzymes can be located in a remarkable diversity of cellular compartments in different organisms. This location does not always reflect their evolutionary origins, as might be expected from the history of their acquisition through endosymbiosis. Instead, the final subcellular localization of the enzyme reflects multiple factors, including evolutionary origin, demand for the product, availability of the substrate, and mechanism of pathway regulation. The biosynthesis of heme in the apicomonad Chromera velia follows a chimeric pathway combining heme elements from the ancient algal symbiont and the host. Computational analyses using different algorithms predict complex targeting patterns, placing enzymes in the mitochondrion, plastid, endoplasmic reticulum, or the cytoplasm. We employed heterologous reporter gene expression in the apicomplexan parasite Toxoplasma gondii and the diatom Phaeodactylum tricornutum to experimentally test these predictions. 5-aminolevulinate synthase was located in the mitochondria in both transfection systems. In T. gondii, the two 5-aminolevulinate dehydratases were located in the cytosol, uroporphyrinogen synthase in the mitochondrion, and the two ferrochelatases in the plastid. In P. tricornutum, all remaining enzymes, from ALA-dehydratase to ferrochelatase, were placed either in the endoplasmic reticulum or in the periplastidial space.

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“…The tetrapyrrole biosynthesis route leading to Chl formation is often referred to as the Mg-branch (for review see Mochizuki et al, 2010 ; Tanaka et al, 2011 ; Tripathy and Pattanayak, 2012 ; Rebeiz, 2014 ; Willows, 2019 ; Bryant et al, 2020 ). Several new data indicate that galactolipids play crucial roles in Chl biosynthesis (Kobayashi et al, 2014 ; Fujii et al, 2019b ) in addition to other factors regulating the Mg-branch at various levels and via different mechanisms as reviewed by Grimm ( 2010 ), Stenbaek and Jensen ( 2010 ), Zhang et al ( 2011 ), Czarnecki and Grimm ( 2012 ), Richter and Grimm ( 2013 ), Brzezowski et al ( 2015 ), Wang and Grimm ( 2015 ), Kobayashi and Masuda ( 2016 ), Yuan et al ( 2017 ), and Herbst et al ( 2019 ).…”

Section: Overview Of the Mg-branch Of Tetrapyrrole Biosynthesismentioning

confidence: 99%

“…Formation of such multi-subunit complexes favors the flow of intermediates during the Chl synthesis in light as well as the inhibition of the process in the dark. Taking into account that FNR1 provides the electrons for the cyclase activity, it is hypothesized that it might also deliver electrons for LPOR and DVR in the multi-enzymatic complex (Herbst et al, 2018(Herbst et al, , 2019. Nevertheless, the direct interaction of YCF54-FNR1 with LPOR and DVR has not yet been shown until now.…”

Section: Late Chlorophyll Biosynthesis Is Associated With Plastid Membranesmentioning

confidence: 99%

The Role of Membranes and Lipid-Protein Interactions in the Mg-Branch of Tetrapyrrole Biosynthesis

Solymosi

Myśliwa-Kurdziel

2021

Front. Plant Sci.

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Chlorophyll (Chl) is essential for photosynthesis and needs to be produced throughout the whole plant life, especially under changing light intensity and stress conditions which may result in the destruction and elimination of these pigments. All steps of the Mg-branch of tetrapyrrole biosynthesis leading to Chl formation are carried out by enzymes associated with plastid membranes. Still the significance of these protein-membrane and protein-lipid interactions in Chl synthesis and chloroplast differentiation are not very well-understood. In this review, we provide an overview on Chl biosynthesis in angiosperms with emphasis on its association with membranes and lipids. Moreover, the last steps of the pathway including the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide), the biosynthesis of the isoprenoid phytyl moiety and the esterification of Chlide are also summarized. The unique biochemical and photophysical properties of the light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) enzyme catalyzing Pchlide photoreduction and located to peculiar tubuloreticular prolamellar body (PLB) membranes of light-deprived tissues of angiosperms and to envelope membranes, as well as to thylakoids (especially grana margins) are also reviewed. Data about the factors influencing tubuloreticular membrane formation within cells, the spectroscopic properties and the in vitro reconstitution of the native LPOR enzyme complexes are also critically discussed.

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Posttranslational control of tetrapyrrole biosynthesis: Interacting proteins, chaperones, auxiliary factors

Cited by 6 publications

References 127 publications

Two chloroplast‐localized MORF proteins act as chaperones to maintain tetrapyrrole biosynthesis

Two chloroplast‐localized MORF proteins act as chaperones to maintain tetrapyrrole biosynthesis

Using Diatom and Apicomplexan Models to Study the Heme Pathway of Chromera velia

The Role of Membranes and Lipid-Protein Interactions in the Mg-Branch of Tetrapyrrole Biosynthesis

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