Differential Operation of Dual Protochlorophyllide Reductases for Chlorophyll Biosynthesis in Response to Environmental Oxygen Levels in the Cyanobacterium <i>Leptolyngbya boryana</i>

Yamazaki, Shoji; Nomata, Jiro; Fujita, Yuichi

doi:10.1104/pp.106.086090

Cited by 101 publications

(93 citation statements)

References 71 publications

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“…Determination of Chl and PC Contents-The concentration of Chl in the 90% methanol extracts from the cells was determined by absorption at 665 nm (model V-550, JASCO, Hachioji, Japan) (19). The amount of Chl was normalized by the optical density at 730 nm (A 730 ; UV1700, Shimadzu, Kyoto, Japan) of the cell suspension used for the extraction.…”

Section: Methodsmentioning

confidence: 99%

MarR-type Transcriptional Regulator ChlR Activates Expression of Tetrapyrrole Biosynthesis Genes in Response to Low-oxygen Conditions in Cyanobacteria

Aoki

Takeda

Omata

et al. 2012

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

MarR-type Transcriptional Regulator ChlR Activates Expression of Tetrapyrrole Biosynthesis Genes in Response to Low-oxygen Conditions in Cyanobacteria

Aoki

Takeda

Omata

et al. 2012

Journal of Biological Chemistry

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“…In this case, POR operates under both aerobic and micro-oxic conditions, but it requires light for its reaction. On the other hand, the Chl BLN complex catalyzes the same reaction only under microoxic conditions, regardless of illumination (28). In contrast, in the case of slr1790, HemY, and HemG homologs, it is difficult to assume any reasons for the presence of slr1790, HemY, or HemG in the bacterial kingdom, as these genes coexist in the same class of bacteria.…”

Section: Discussionmentioning

confidence: 93%

“…Such occurrence of multiple enzymes is not rare in the tetrapyrrole biosynthetic pathway (24). For example, reduction of protochlorophyllide is catalyzed by two distinct enzymes, POR and the Chl BLN complex, in cyanobacteria (28). In this case, POR operates under both aerobic and micro-oxic conditions, but it requires light for its reaction.…”

Section: Discussionmentioning

confidence: 99%

Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC6803

Kato

Tanaka

Sano

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Protoporphyrinogen oxidase (Protox) catalyses the oxidation of protoporphyrinogen IX to protoporphyrin IX during the synthesis of tetrapyrrole molecules. Protox is encoded by the hemY gene in eukaryotes and by the hemG gene in many γ-proteobacteria, including Escherichia coli. It has been suggested that other bacteria possess a yet unidentified type of Protox. To identify a unique bacterial gene encoding Protox, we first introduced the Arabidopsis hemY gene into the genome of the cyanobacterium, Synechocystis sp. PCC6803. We subsequently mutagenized the cells by transposon tagging and screened the tagged lines for mutants that were sensitive to acifluorfen, which is a specific inhibitor of the hemY-type Protox. Several cell lines containing the tagged slr1790 locus exhibited acifluorfen sensitivity. The slr1790 gene encodes a putative membrane-spanning protein that is distantly related to the M subunit of NADH dehydrogenase complex I. We attempted to disrupt this gene in the wild-type background of Synechocystis, but we were only able to obtain heteroplasmic disruptants. These cells accumulated a substantial amount of protoporphyrin IX, suggesting that the slr1790 gene is essential for growth and Protox activity of cells. We found that most cyanobacteria and many other bacteria possess slr1790 homologs. We overexpressed an slr1790 homolog of Rhodobacter sphaeroides in Escherichia coli and found that this recombinant protein possesses Protox activity in vitro. These results collectively demonstrate that slr1790 encodes a unique Protox enzyme and we propose naming the slr1790 gene “hemJ.

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“…Determination of Chl Contents-The concentration of Chl in the 90% methanol extracts from the cells was determined by absorption at 665 nm (model V-550, JASCO, Hachioji, Japan) (27). The amount of Chl was normalized by the optical density at 730 nm (UV1700, Shimadzu, Kyoto, Japan) of the cell suspension used for the extraction.…”

Section: Methodsmentioning

confidence: 99%

A Novel “Oxygen-induced” Greening Process in a Cyanobacterial Mutant Lacking the Transcriptional Activator ChlR Involved in Low-oxygen Adaptation of Tetrapyrrole Biosynthesis

Aoki¹,

Hiraide

Yamakawa

et al. 2014

Journal of Biological Chemistry

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Background: ChlR activates the transcription of genes encoding low-oxygen-type enzymes in response to hypoxia in cyanobacteria. Results:The chlR-lacking mutant showed a novel "oxygen-induced" greening process upon exposure to air. Conclusion: The contents of photosystems were correlated well with the chlorophyll contents in the greening process. Significance: Oxygen-induced greening provides a promising alternative system to investigate the biogenesis of photosystems.

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Differential Operation of Dual Protochlorophyllide Reductases for Chlorophyll Biosynthesis in Response to Environmental Oxygen Levels in the Cyanobacterium Leptolyngbya boryana

Cited by 101 publications

References 71 publications

MarR-type Transcriptional Regulator ChlR Activates Expression of Tetrapyrrole Biosynthesis Genes in Response to Low-oxygen Conditions in Cyanobacteria

MarR-type Transcriptional Regulator ChlR Activates Expression of Tetrapyrrole Biosynthesis Genes in Response to Low-oxygen Conditions in Cyanobacteria

Identification of a gene essential for protoporphyrinogen IX oxidase activity in the cyanobacterium Synechocystis sp. PCC6803

A Novel “Oxygen-induced” Greening Process in a Cyanobacterial Mutant Lacking the Transcriptional Activator ChlR Involved in Low-oxygen Adaptation of Tetrapyrrole Biosynthesis

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