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  LCAA, a Novel Factor Required for Magnesium Protoporphyrin Monomethylester Cyclase Accumulation and Feedback Control of Aminolevulinic Acid Biosynthesis in Tobacco

Albus, C. A., Salinas, A., Czarnecki, O., Kahlau, S., Rothbart, M., Thiele, W., et al. (2012). LCAA, a Novel Factor Required for Magnesium Protoporphyrin Monomethylester Cyclase Accumulation and Feedback Control of Aminolevulinic Acid Biosynthesis in Tobacco. Plant Physiology, 160(4), 1923-1939. doi:10.1104/pp.112.206045.

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Albus-2012-LCAA, a Novel Factor.pdf
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 Creators:
Albus, C. A.1, Author           
Salinas, A.2, Author
Czarnecki, O.2, Author
Kahlau, S.1, Author           
Rothbart, M.2, Author
Thiele, W.1, Author           
Lein, W.3, Author           
Bock, R.1, Author           
Grimm, B.2, Author
Schöttler, M. A.4, Author           
Affiliations:
1Organelle Biology and Biotechnology, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753326              
2External Organizations, ou_persistent22              
3Gene Function, Department Stitt, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753333              
4Photosynthesis Research, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753323              

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Free keywords: light-harvesting complex ester oxidative cyclase a/b-binding proteins arabidopsis-thaliana tetrapyrrole biosynthesis photosystem-ii chlorophyll biosynthesis antisense inhibition nicotiana-tabacum gene-expression
 Abstract: Low Chlorophyll Accumulation A (LCAA) antisense plants were obtained from a screen for genes whose partial down-regulation results in a strong chlorophyll deficiency in tobacco (Nicotiana tabacum). The LCAA mutants are affected in a plastid-localized protein of unknown function, which is conserved in cyanobacteria and all photosynthetic eukaryotes. They suffer from drastically reduced light-harvesting complex (LHC) contents, while the accumulation of all other photosynthetic complexes per leaf area is less affected. As the disturbed accumulation of LHC proteins could be either attributable to a defect in LHC biogenesis itself or to a bottleneck in chlorophyll biosynthesis, chlorophyll synthesis rates and chlorophyll synthesis intermediates were measured. LCAA antisense plants accumulate magnesium (Mg) protoporphyrin monomethylester and contain reduced protochlorophyllide levels and a reduced content of CHL27, a subunit of the Mg protoporphyrin monomethylester cyclase. Bimolecular fluorescence complementation assays confirm a direct interaction between LCAA and CHL27. 5-Aminolevulinic acid synthesis rates are increased and correlate with an increased content of glutamyl-transfer RNA reductase. We suggest that LCAA encodes an additional subunit of the Mg protoporphyrin monomethylester cyclase, is required for the stability of CHL27, and contributes to feedback-control of 5-aminolevulinic acid biosynthesis, the rate-limiting step of chlorophyll biosynthesis.

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Language(s): eng - English
 Dates: 2012
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: ISI:000311998200021
DOI: 10.1104/pp.112.206045
ISSN: 0032-0889
URI: ://000311998200021http://www.plantphysiol.org/content/160/4/1923.full.pdf
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Title: Plant Physiology
  Other : Plant Physiol.
Source Genre: Journal
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Publ. Info: Bethesda, Md. : American Society of Plant Biologists
Pages: - Volume / Issue: 160 (4) Sequence Number: - Start / End Page: 1923 - 1939 Identifier: ISSN: 0032-0889
CoNE: https://pure.mpg.de/cone/journals/resource/991042744294438