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Bundle sheath suberisation is required for C4 photosynthesis in a Setaria viridis mutant
C 4 photosynthesis provides an effective solution for overcoming the catalytic inefficiency of Rubisco. The pathway is characterised by a biochemical CO 2 concentrating mechanism that operates across mesophyll and bundle sheath (BS) cells and relies on a gas tight BS compartment. A screen of a mutan...
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Published in: | Communications biology 2021-02, Vol.4 (1), p.254-254, Article 254 |
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description | C
4
photosynthesis provides an effective solution for overcoming the catalytic inefficiency of Rubisco. The pathway is characterised by a biochemical CO
2
concentrating mechanism that operates across mesophyll and bundle sheath (BS) cells and relies on a gas tight BS compartment. A screen of a mutant population of
Setaria viridis
, an NADP-malic enzyme type C
4
monocot, generated using N-nitroso-N-methylurea identified a mutant with an amino acid change in the gene coding region of the ABCG transporter, a step in the suberin synthesis pathway. Here, Nile red staining, TEM, and GC/MS confirmed the alteration in suberin deposition in the BS cell wall of the mutant. We show that this has disrupted the suberin lamellae of BS cell wall and increased BS conductance to CO
2
diffusion more than two-fold in the mutant. Consequently, BS CO
2
partial pressure is reduced and CO
2
assimilation was impaired in the mutant. Our findings provide experimental evidence that a functional suberin lamellae is an essential anatomical feature for efficient C
4
photosynthesis in NADP-ME plants like
S. viridis
and have implications for engineering strategies to ensure future food security.
Florence Danila et al. perform mutation screens on
Setaria viridis
and identify an ABCG transporter gene which serves as a step in the suberin synthesis pathway. This study demonstrates that a functional suberin lamellae is essential for efficient C
4
photosynthesis in
S. viridis
. |
doi_str_mv | 10.1038/s42003-021-01772-4 |
format | article |
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4
photosynthesis provides an effective solution for overcoming the catalytic inefficiency of Rubisco. The pathway is characterised by a biochemical CO
2
concentrating mechanism that operates across mesophyll and bundle sheath (BS) cells and relies on a gas tight BS compartment. A screen of a mutant population of
Setaria viridis
, an NADP-malic enzyme type C
4
monocot, generated using N-nitroso-N-methylurea identified a mutant with an amino acid change in the gene coding region of the ABCG transporter, a step in the suberin synthesis pathway. Here, Nile red staining, TEM, and GC/MS confirmed the alteration in suberin deposition in the BS cell wall of the mutant. We show that this has disrupted the suberin lamellae of BS cell wall and increased BS conductance to CO
2
diffusion more than two-fold in the mutant. Consequently, BS CO
2
partial pressure is reduced and CO
2
assimilation was impaired in the mutant. Our findings provide experimental evidence that a functional suberin lamellae is an essential anatomical feature for efficient C
4
photosynthesis in NADP-ME plants like
S. viridis
and have implications for engineering strategies to ensure future food security.
Florence Danila et al. perform mutation screens on
Setaria viridis
and identify an ABCG transporter gene which serves as a step in the suberin synthesis pathway. This study demonstrates that a functional suberin lamellae is essential for efficient C
4
photosynthesis in
S. viridis
.</description><identifier>ISSN: 2399-3642</identifier><identifier>EISSN: 2399-3642</identifier><identifier>DOI: 10.1038/s42003-021-01772-4</identifier><identifier>PMID: 33637850</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14/19 ; 14/28 ; 45/23 ; 631/449/1734/2689 ; 706/1143 ; 82/16 ; 82/58 ; Amino acids ; Biology ; Biomedical and Life Sciences ; Carbon dioxide ; Cell walls ; Conductance ; Food security ; Lamellae ; Life Sciences ; Malic enzyme ; Mesophyll ; Mutants ; N-Methyl-N-nitrosourea ; NADP ; Photosynthesis ; Ribulose-bisphosphate carboxylase ; Setaria viridis</subject><ispartof>Communications biology, 2021-02, Vol.4 (1), p.254-254, Article 254</ispartof><rights>The Author(s) 2021</rights><rights>The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4324-eb44c0a0e9db5906a4e260ff945dc24aeafa71a1cc1d4e2e5aea0bad714a86093</citedby><cites>FETCH-LOGICAL-c4324-eb44c0a0e9db5906a4e260ff945dc24aeafa71a1cc1d4e2e5aea0bad714a86093</cites><orcidid>0000-0002-8523-0256 ; 0000-0002-8366-2071 ; 0000-0002-7352-3852</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7910553/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2493701865?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768</link.rule.ids></links><search><creatorcontrib>Danila, Florence R.</creatorcontrib><creatorcontrib>Thakur, Vivek</creatorcontrib><creatorcontrib>Chatterjee, Jolly</creatorcontrib><creatorcontrib>Bala, Soumi</creatorcontrib><creatorcontrib>Coe, Robert A.</creatorcontrib><creatorcontrib>Acebron, Kelvin</creatorcontrib><creatorcontrib>Furbank, Robert T.</creatorcontrib><creatorcontrib>von Caemmerer, Susanne</creatorcontrib><creatorcontrib>Quick, William Paul</creatorcontrib><title>Bundle sheath suberisation is required for C4 photosynthesis in a Setaria viridis mutant</title><title>Communications biology</title><addtitle>Commun Biol</addtitle><description>C
4
photosynthesis provides an effective solution for overcoming the catalytic inefficiency of Rubisco. The pathway is characterised by a biochemical CO
2
concentrating mechanism that operates across mesophyll and bundle sheath (BS) cells and relies on a gas tight BS compartment. A screen of a mutant population of
Setaria viridis
, an NADP-malic enzyme type C
4
monocot, generated using N-nitroso-N-methylurea identified a mutant with an amino acid change in the gene coding region of the ABCG transporter, a step in the suberin synthesis pathway. Here, Nile red staining, TEM, and GC/MS confirmed the alteration in suberin deposition in the BS cell wall of the mutant. We show that this has disrupted the suberin lamellae of BS cell wall and increased BS conductance to CO
2
diffusion more than two-fold in the mutant. Consequently, BS CO
2
partial pressure is reduced and CO
2
assimilation was impaired in the mutant. Our findings provide experimental evidence that a functional suberin lamellae is an essential anatomical feature for efficient C
4
photosynthesis in NADP-ME plants like
S. viridis
and have implications for engineering strategies to ensure future food security.
Florence Danila et al. perform mutation screens on
Setaria viridis
and identify an ABCG transporter gene which serves as a step in the suberin synthesis pathway. This study demonstrates that a functional suberin lamellae is essential for efficient C
4
photosynthesis in
S. viridis
.</description><subject>14/19</subject><subject>14/28</subject><subject>45/23</subject><subject>631/449/1734/2689</subject><subject>706/1143</subject><subject>82/16</subject><subject>82/58</subject><subject>Amino acids</subject><subject>Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Carbon dioxide</subject><subject>Cell walls</subject><subject>Conductance</subject><subject>Food security</subject><subject>Lamellae</subject><subject>Life Sciences</subject><subject>Malic enzyme</subject><subject>Mesophyll</subject><subject>Mutants</subject><subject>N-Methyl-N-nitrosourea</subject><subject>NADP</subject><subject>Photosynthesis</subject><subject>Ribulose-bisphosphate carboxylase</subject><subject>Setaria viridis</subject><issn>2399-3642</issn><issn>2399-3642</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNp9kkuLFDEUhQtRnGGcP-Aq4MZN6c2jHtkI2vgYGHChgrtwk9zqTlNd6UmqBubfm54a1HHhKuGecz4ul1NVLzm84SD7t1kJAFmD4DXwrhO1elKdC6l1LVslnv71P6suc94DANdat1I9r86kbGXXN3Be_fywTH4klneE847lxVIKGecQJxYyS3SzhESeDTGxjWLHXZxjvpvmHeUih4kh-0YzpoDsNqTgy_CwzDjNL6pnA46ZLh_ei-rHp4_fN1_q66-frzbvr2unpFA1WaUcIJD2ttHQoiLRwjBo1XgnFBIO2HHkznFfJGrKBCz6jivsW9DyorpauT7i3hxTOGC6MxGDuR_EtDWY5uBGMhJcI4HsYC1XNJRrdKh76_0AaBGbwnq3so6LPZB3NM0Jx0fQx8oUdmYbb02nOTSNLIDXD4AUbxbKszmE7GgccaK4ZCOUVhKEbnmxvvrHuo9LmsqpTi7ZAe_b00ZidbkUc040_F6Ggzn1wKw9MKUH5r4HRpWQXEO5mKctpT_o_6R-AS5Gtfg</recordid><startdate>20210226</startdate><enddate>20210226</enddate><creator>Danila, Florence R.</creator><creator>Thakur, Vivek</creator><creator>Chatterjee, Jolly</creator><creator>Bala, Soumi</creator><creator>Coe, Robert A.</creator><creator>Acebron, Kelvin</creator><creator>Furbank, Robert T.</creator><creator>von Caemmerer, Susanne</creator><creator>Quick, William Paul</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><general>Nature Portfolio</general><scope>C6C</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7XB</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-8523-0256</orcidid><orcidid>https://orcid.org/0000-0002-8366-2071</orcidid><orcidid>https://orcid.org/0000-0002-7352-3852</orcidid></search><sort><creationdate>20210226</creationdate><title>Bundle sheath suberisation is required for C4 photosynthesis in a Setaria viridis mutant</title><author>Danila, Florence R. ; 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4
photosynthesis provides an effective solution for overcoming the catalytic inefficiency of Rubisco. The pathway is characterised by a biochemical CO
2
concentrating mechanism that operates across mesophyll and bundle sheath (BS) cells and relies on a gas tight BS compartment. A screen of a mutant population of
Setaria viridis
, an NADP-malic enzyme type C
4
monocot, generated using N-nitroso-N-methylurea identified a mutant with an amino acid change in the gene coding region of the ABCG transporter, a step in the suberin synthesis pathway. Here, Nile red staining, TEM, and GC/MS confirmed the alteration in suberin deposition in the BS cell wall of the mutant. We show that this has disrupted the suberin lamellae of BS cell wall and increased BS conductance to CO
2
diffusion more than two-fold in the mutant. Consequently, BS CO
2
partial pressure is reduced and CO
2
assimilation was impaired in the mutant. Our findings provide experimental evidence that a functional suberin lamellae is an essential anatomical feature for efficient C
4
photosynthesis in NADP-ME plants like
S. viridis
and have implications for engineering strategies to ensure future food security.
Florence Danila et al. perform mutation screens on
Setaria viridis
and identify an ABCG transporter gene which serves as a step in the suberin synthesis pathway. This study demonstrates that a functional suberin lamellae is essential for efficient C
4
photosynthesis in
S. viridis
.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>33637850</pmid><doi>10.1038/s42003-021-01772-4</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-8523-0256</orcidid><orcidid>https://orcid.org/0000-0002-8366-2071</orcidid><orcidid>https://orcid.org/0000-0002-7352-3852</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 14/19 14/28 45/23 631/449/1734/2689 706/1143 82/16 82/58 Amino acids Biology Biomedical and Life Sciences Carbon dioxide Cell walls Conductance Food security Lamellae Life Sciences Malic enzyme Mesophyll Mutants N-Methyl-N-nitrosourea NADP Photosynthesis Ribulose-bisphosphate carboxylase Setaria viridis |
title | Bundle sheath suberisation is required for C4 photosynthesis in a Setaria viridis mutant |
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