Bilin-dependent regulation of chlorophyll biosynthesis by GUN4
Biosyntheses of chlorophyll and heme in oxygenic phototrophs share a common trunk pathway that diverges with insertion of magnesium or iron into the last common intermediate, protoporphyrin IX. Since both tetrapyrroles are pro-oxidants, it is essential that their metabolism is tightly regulated. Her...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2021-05, Vol.118 (20), p.1-9 |
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| creator | Zhang, Weiqing Willows, Robert D. Deng, Rui Li, Zheng Li, Mengqi Wang, Yan Guo, Yunling Shi, Weida Fan, Qiuling Martin, Shelley S. Rockwell, Nathan C. Lagarias, J. Clark Duanmu, Deqiang |
| description | Biosyntheses of chlorophyll and heme in oxygenic phototrophs share a common trunk pathway that diverges with insertion of magnesium or iron into the last common intermediate, protoporphyrin IX. Since both tetrapyrroles are pro-oxidants, it is essential that their metabolism is tightly regulated. Here, we establish that heme-derived linear tetrapyrroles (bilins) function to stimulate the enzymatic activity of magnesium chelatase (MgCh) via their interaction with GENOMES UNCOUPLED 4 (GUN4) in the model green alga Chlamydomonas reinhardtii. A key tetrapyrrole-binding component of MgCh found in all oxygenic photosynthetic species, CrGUN4, also stabilizes the bilin-dependent accumulation of protoporphyrin IX-binding CrCHLH1 subunit of MgCh in light-grown C. reinhardtii cells by preventing its photooxidative inactivation. Exogenous application of biliverdin IXα reverses the loss of CrCHLH1 in the bilin-deficient heme oxygenase (hmox1) mutant, but not in the gun4 mutant. We propose that these dual regulatory roles of GUN4: bilin complexes are responsible for the retention of bilin biosynthesis in all photosynthetic eukaryotes, which sustains chlorophyll biosynthesis in an illuminated oxic environment. |
| doi_str_mv | 10.1073/pnas.2104443118 |
| format | Article |
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Clark ; Duanmu, Deqiang</creator><creatorcontrib>Zhang, Weiqing ; Willows, Robert D. ; Deng, Rui ; Li, Zheng ; Li, Mengqi ; Wang, Yan ; Guo, Yunling ; Shi, Weida ; Fan, Qiuling ; Martin, Shelley S. ; Rockwell, Nathan C. ; Lagarias, J. Clark ; Duanmu, Deqiang ; Univ. of California, Davis, CA (United States)</creatorcontrib><description>Biosyntheses of chlorophyll and heme in oxygenic phototrophs share a common trunk pathway that diverges with insertion of magnesium or iron into the last common intermediate, protoporphyrin IX. Since both tetrapyrroles are pro-oxidants, it is essential that their metabolism is tightly regulated. Here, we establish that heme-derived linear tetrapyrroles (bilins) function to stimulate the enzymatic activity of magnesium chelatase (MgCh) via their interaction with GENOMES UNCOUPLED 4 (GUN4) in the model green alga Chlamydomonas reinhardtii. A key tetrapyrrole-binding component of MgCh found in all oxygenic photosynthetic species, CrGUN4, also stabilizes the bilin-dependent accumulation of protoporphyrin IX-binding CrCHLH1 subunit of MgCh in light-grown C. reinhardtii cells by preventing its photooxidative inactivation. Exogenous application of biliverdin IXα reverses the loss of CrCHLH1 in the bilin-deficient heme oxygenase (hmox1) mutant, but not in the gun4 mutant. We propose that these dual regulatory roles of GUN4: bilin complexes are responsible for the retention of bilin biosynthesis in all photosynthetic eukaryotes, which sustains chlorophyll biosynthesis in an illuminated oxic environment.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.2104443118</identifier><identifier>PMID: 33975960</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Aquatic plants ; BASIC BIOLOGICAL SCIENCES ; bilin reductase ; bilin reductase chlamydomonas chlorophyll biosynthesis heme oxygenase photosynthesis phycocyanobilin reactive oxygen species ; Biliverdin ; Binding ; Biological Sciences ; Biosynthesis ; Chlorophyll ; Enzymatic activity ; Eukaryotes ; Genomes ; Heme ; heme oxygenase ; Inactivation ; Magnesium ; Mutants ; Oxidants ; Oxidizing agents ; Oxygenase ; Photosynthesis ; phycocyanobilin ; Protoporphyrin ; Protoporphyrin IX ; reactive oxygen species ; science & technology ; Tetrapyrroles</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2021-05, Vol.118 (20), p.1-9</ispartof><rights>Copyright National Academy of Sciences May 18, 2021</rights><rights>2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-f895c72aa8100acdadd7e3b4d45f291ae22a23b16539721434b991520f39c5c3</citedby><cites>FETCH-LOGICAL-c470t-f895c72aa8100acdadd7e3b4d45f291ae22a23b16539721434b991520f39c5c3</cites><orcidid>0000-0003-2428-1209 ; 0000-0002-7748-7019 ; 0000-0002-2093-0403 ; 0000-0001-7530-0268 ; 0000-0002-0731-2950 ; 0000-0002-9365-362X ; 0000000207312950 ; 0000000175300268 ; 000000029365362X ; 0000000220930403 ; 0000000277487019 ; 0000000324281209</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/27040446$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/27040446$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33975960$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1847981$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Weiqing</creatorcontrib><creatorcontrib>Willows, Robert D.</creatorcontrib><creatorcontrib>Deng, Rui</creatorcontrib><creatorcontrib>Li, Zheng</creatorcontrib><creatorcontrib>Li, Mengqi</creatorcontrib><creatorcontrib>Wang, Yan</creatorcontrib><creatorcontrib>Guo, Yunling</creatorcontrib><creatorcontrib>Shi, Weida</creatorcontrib><creatorcontrib>Fan, Qiuling</creatorcontrib><creatorcontrib>Martin, Shelley S.</creatorcontrib><creatorcontrib>Rockwell, Nathan C.</creatorcontrib><creatorcontrib>Lagarias, J. Clark</creatorcontrib><creatorcontrib>Duanmu, Deqiang</creatorcontrib><creatorcontrib>Univ. of California, Davis, CA (United States)</creatorcontrib><title>Bilin-dependent regulation of chlorophyll biosynthesis by GUN4</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Biosyntheses of chlorophyll and heme in oxygenic phototrophs share a common trunk pathway that diverges with insertion of magnesium or iron into the last common intermediate, protoporphyrin IX. Since both tetrapyrroles are pro-oxidants, it is essential that their metabolism is tightly regulated. Here, we establish that heme-derived linear tetrapyrroles (bilins) function to stimulate the enzymatic activity of magnesium chelatase (MgCh) via their interaction with GENOMES UNCOUPLED 4 (GUN4) in the model green alga Chlamydomonas reinhardtii. A key tetrapyrrole-binding component of MgCh found in all oxygenic photosynthetic species, CrGUN4, also stabilizes the bilin-dependent accumulation of protoporphyrin IX-binding CrCHLH1 subunit of MgCh in light-grown C. reinhardtii cells by preventing its photooxidative inactivation. Exogenous application of biliverdin IXα reverses the loss of CrCHLH1 in the bilin-deficient heme oxygenase (hmox1) mutant, but not in the gun4 mutant. We propose that these dual regulatory roles of GUN4: bilin complexes are responsible for the retention of bilin biosynthesis in all photosynthetic eukaryotes, which sustains chlorophyll biosynthesis in an illuminated oxic environment.</description><subject>Aquatic plants</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>bilin reductase</subject><subject>bilin reductase chlamydomonas chlorophyll biosynthesis heme oxygenase photosynthesis phycocyanobilin reactive oxygen species</subject><subject>Biliverdin</subject><subject>Binding</subject><subject>Biological Sciences</subject><subject>Biosynthesis</subject><subject>Chlorophyll</subject><subject>Enzymatic activity</subject><subject>Eukaryotes</subject><subject>Genomes</subject><subject>Heme</subject><subject>heme oxygenase</subject><subject>Inactivation</subject><subject>Magnesium</subject><subject>Mutants</subject><subject>Oxidants</subject><subject>Oxidizing agents</subject><subject>Oxygenase</subject><subject>Photosynthesis</subject><subject>phycocyanobilin</subject><subject>Protoporphyrin</subject><subject>Protoporphyrin IX</subject><subject>reactive oxygen species</subject><subject>science & technology</subject><subject>Tetrapyrroles</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNpdkc1v1DAQxS0EokvhzAkUwYVL2hnbieNLJaigIFVwKWfLcZzGq6wdbAdp_3u82rJ8nOYwv3nzZh4hLxEuEAS7XLxOFxSBc84Qu0dkgyCxbrmEx2QDQEXdccrPyLOUtgAgmw6ekjPGpGhkCxty9cHNzteDXawfrM9VtPfrrLMLvgpjZaY5xLBM-3muehfS3ufJJpeqfl_dfP_Kn5Mno56TffFQz8ndp49315_r2283X67f39aGC8j12MnGCKp1hwDaDHoYhGU9H3gzUonaUqop67FtijGKnPFeSmwojEyaxrBzcnWUXdZ-ZwdTjEY9qyW6nY57FbRT_3a8m9R9-Kk6LAdTLAJvjgIhZaeScdmayQTvrckKOy5kd4DePWyJ4cdqU1Y7l4ydZ-1tWJOiDW2RSRSyoG__Q7dhjb68oFAMGuS8PVCXR8rEkFK048kxgjrkpw75qT_5lYnXfx964n8HVoBXR2CbcoinPhXAi0jLfgF5PJ9W</recordid><startdate>20210518</startdate><enddate>20210518</enddate><creator>Zhang, Weiqing</creator><creator>Willows, Robert D.</creator><creator>Deng, Rui</creator><creator>Li, Zheng</creator><creator>Li, Mengqi</creator><creator>Wang, Yan</creator><creator>Guo, Yunling</creator><creator>Shi, Weida</creator><creator>Fan, Qiuling</creator><creator>Martin, Shelley S.</creator><creator>Rockwell, Nathan C.</creator><creator>Lagarias, J. Clark</creator><creator>Duanmu, Deqiang</creator><general>National Academy of Sciences</general><general>Proceedings of the National Academy of Sciences</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-2428-1209</orcidid><orcidid>https://orcid.org/0000-0002-7748-7019</orcidid><orcidid>https://orcid.org/0000-0002-2093-0403</orcidid><orcidid>https://orcid.org/0000-0001-7530-0268</orcidid><orcidid>https://orcid.org/0000-0002-0731-2950</orcidid><orcidid>https://orcid.org/0000-0002-9365-362X</orcidid><orcidid>https://orcid.org/0000000207312950</orcidid><orcidid>https://orcid.org/0000000175300268</orcidid><orcidid>https://orcid.org/000000029365362X</orcidid><orcidid>https://orcid.org/0000000220930403</orcidid><orcidid>https://orcid.org/0000000277487019</orcidid><orcidid>https://orcid.org/0000000324281209</orcidid></search><sort><creationdate>20210518</creationdate><title>Bilin-dependent regulation of chlorophyll biosynthesis by GUN4</title><author>Zhang, Weiqing ; Willows, Robert D. ; Deng, Rui ; Li, Zheng ; Li, Mengqi ; Wang, Yan ; Guo, Yunling ; Shi, Weida ; Fan, Qiuling ; Martin, Shelley S. ; Rockwell, Nathan C. ; Lagarias, J. 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Clark</creatorcontrib><creatorcontrib>Duanmu, Deqiang</creatorcontrib><creatorcontrib>Univ. of California, Davis, CA (United States)</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Weiqing</au><au>Willows, Robert D.</au><au>Deng, Rui</au><au>Li, Zheng</au><au>Li, Mengqi</au><au>Wang, Yan</au><au>Guo, Yunling</au><au>Shi, Weida</au><au>Fan, Qiuling</au><au>Martin, Shelley S.</au><au>Rockwell, Nathan C.</au><au>Lagarias, J. Clark</au><au>Duanmu, Deqiang</au><aucorp>Univ. of California, Davis, CA (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bilin-dependent regulation of chlorophyll biosynthesis by GUN4</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2021-05-18</date><risdate>2021</risdate><volume>118</volume><issue>20</issue><spage>1</spage><epage>9</epage><pages>1-9</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Biosyntheses of chlorophyll and heme in oxygenic phototrophs share a common trunk pathway that diverges with insertion of magnesium or iron into the last common intermediate, protoporphyrin IX. Since both tetrapyrroles are pro-oxidants, it is essential that their metabolism is tightly regulated. Here, we establish that heme-derived linear tetrapyrroles (bilins) function to stimulate the enzymatic activity of magnesium chelatase (MgCh) via their interaction with GENOMES UNCOUPLED 4 (GUN4) in the model green alga Chlamydomonas reinhardtii. A key tetrapyrrole-binding component of MgCh found in all oxygenic photosynthetic species, CrGUN4, also stabilizes the bilin-dependent accumulation of protoporphyrin IX-binding CrCHLH1 subunit of MgCh in light-grown C. reinhardtii cells by preventing its photooxidative inactivation. Exogenous application of biliverdin IXα reverses the loss of CrCHLH1 in the bilin-deficient heme oxygenase (hmox1) mutant, but not in the gun4 mutant. We propose that these dual regulatory roles of GUN4: bilin complexes are responsible for the retention of bilin biosynthesis in all photosynthetic eukaryotes, which sustains chlorophyll biosynthesis in an illuminated oxic environment.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>33975960</pmid><doi>10.1073/pnas.2104443118</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-2428-1209</orcidid><orcidid>https://orcid.org/0000-0002-7748-7019</orcidid><orcidid>https://orcid.org/0000-0002-2093-0403</orcidid><orcidid>https://orcid.org/0000-0001-7530-0268</orcidid><orcidid>https://orcid.org/0000-0002-0731-2950</orcidid><orcidid>https://orcid.org/0000-0002-9365-362X</orcidid><orcidid>https://orcid.org/0000000207312950</orcidid><orcidid>https://orcid.org/0000000175300268</orcidid><orcidid>https://orcid.org/000000029365362X</orcidid><orcidid>https://orcid.org/0000000220930403</orcidid><orcidid>https://orcid.org/0000000277487019</orcidid><orcidid>https://orcid.org/0000000324281209</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Aquatic plants BASIC BIOLOGICAL SCIENCES bilin reductase bilin reductase chlamydomonas chlorophyll biosynthesis heme oxygenase photosynthesis phycocyanobilin reactive oxygen species Biliverdin Binding Biological Sciences Biosynthesis Chlorophyll Enzymatic activity Eukaryotes Genomes Heme heme oxygenase Inactivation Magnesium Mutants Oxidants Oxidizing agents Oxygenase Photosynthesis phycocyanobilin Protoporphyrin Protoporphyrin IX reactive oxygen species science & technology Tetrapyrroles |
| title | Bilin-dependent regulation of chlorophyll biosynthesis by GUN4 |
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