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Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria

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Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria. / Whitney, Spencer M.; Sharwood, Robert E.; Orr, Douglas et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, No. 35, 30.08.2011, p. 14688-14693.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Whitney, SM, Sharwood, RE, Orr, D, White, SJ, Alonso, H & Galmés, J 2011, 'Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria', Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 35, pp. 14688-14693. https://doi.org/10.1073/pnas.1109503108

APA

Whitney, S. M., Sharwood, R. E., Orr, D., White, S. J., Alonso, H., & Galmés, J. (2011). Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria. Proceedings of the National Academy of Sciences of the United States of America, 108(35), 14688-14693. https://doi.org/10.1073/pnas.1109503108

Vancouver

Whitney SM, Sharwood RE, Orr D, White SJ, Alonso H, Galmés J. Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria. Proceedings of the National Academy of Sciences of the United States of America. 2011 Aug 30;108(35):14688-14693. doi: 10.1073/pnas.1109503108

Author

Whitney, Spencer M. ; Sharwood, Robert E. ; Orr, Douglas et al. / Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria. In: Proceedings of the National Academy of Sciences of the United States of America. 2011 ; Vol. 108, No. 35. pp. 14688-14693.

Bibtex

@article{9b850dfc262d467cba7addded94ec371,
title = "Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria",
abstract = "Improving global yields of important agricultural crops is a complex challenge. Enhancing yield and resource use by engineering improvements to photosynthetic carbon assimilation is one potential solution. During the last 40 million years C 4 photosynthesis has evolved multiple times, enabling plants to evade the catalytic inadequacies of the CO 2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco). Compared with their C 3 ancestors, C 4 plants combine a faster rubisco with a biochemical CO 2- concentrating mechanism, enabling more efficient use of water and nitrogen and enhanced yield. Here we show the versatility of plastome manipulation in tobacco for identifying sequences in C 4-rubisco that can be transplanted into C 3-rubisco to improve carboxylation rate (V C). Using transplastomic tobacco lines expressing native and mutated rubisco large subunits (L-subunits) from Flaveria pringlei (C 3), Flaveria floridana (C 3-C 4), and Flaveria bidentis (C 4), we reveal that Met-309-Ile substitutions in the L-subunit act as a catalytic switch between C 4 ( 309Ile; faster V C, lower CO 2 affinity) and C 3 ( 309Met; slower VC, higher CO 2 affinity) catalysis. Application of this transplastomic system permits further identification of other structural solutions selected by nature that can increase rubisco V C in C 3 crops. Coengineering a catalytically faster C 3 rubisco and a CO 2-concentrating mechanism within C 3 crop species could enhance their efficiency in resource use and yield.",
keywords = "Chloroplast transformation, CO assimilation, Gas exchange, rbcL mutagenesis",
author = "Whitney, {Spencer M.} and Sharwood, {Robert E.} and Douglas Orr and White, {Sarah J.} and Hernan Alonso and Jeroni Galm{\'e}s",
year = "2011",
month = aug,
day = "30",
doi = "10.1073/pnas.1109503108",
language = "English",
volume = "108",
pages = "14688--14693",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "35",

}

RIS

TY - JOUR

T1 - Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in flaveria

AU - Whitney, Spencer M.

AU - Sharwood, Robert E.

AU - Orr, Douglas

AU - White, Sarah J.

AU - Alonso, Hernan

AU - Galmés, Jeroni

PY - 2011/8/30

Y1 - 2011/8/30

N2 - Improving global yields of important agricultural crops is a complex challenge. Enhancing yield and resource use by engineering improvements to photosynthetic carbon assimilation is one potential solution. During the last 40 million years C 4 photosynthesis has evolved multiple times, enabling plants to evade the catalytic inadequacies of the CO 2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco). Compared with their C 3 ancestors, C 4 plants combine a faster rubisco with a biochemical CO 2- concentrating mechanism, enabling more efficient use of water and nitrogen and enhanced yield. Here we show the versatility of plastome manipulation in tobacco for identifying sequences in C 4-rubisco that can be transplanted into C 3-rubisco to improve carboxylation rate (V C). Using transplastomic tobacco lines expressing native and mutated rubisco large subunits (L-subunits) from Flaveria pringlei (C 3), Flaveria floridana (C 3-C 4), and Flaveria bidentis (C 4), we reveal that Met-309-Ile substitutions in the L-subunit act as a catalytic switch between C 4 ( 309Ile; faster V C, lower CO 2 affinity) and C 3 ( 309Met; slower VC, higher CO 2 affinity) catalysis. Application of this transplastomic system permits further identification of other structural solutions selected by nature that can increase rubisco V C in C 3 crops. Coengineering a catalytically faster C 3 rubisco and a CO 2-concentrating mechanism within C 3 crop species could enhance their efficiency in resource use and yield.

AB - Improving global yields of important agricultural crops is a complex challenge. Enhancing yield and resource use by engineering improvements to photosynthetic carbon assimilation is one potential solution. During the last 40 million years C 4 photosynthesis has evolved multiple times, enabling plants to evade the catalytic inadequacies of the CO 2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco). Compared with their C 3 ancestors, C 4 plants combine a faster rubisco with a biochemical CO 2- concentrating mechanism, enabling more efficient use of water and nitrogen and enhanced yield. Here we show the versatility of plastome manipulation in tobacco for identifying sequences in C 4-rubisco that can be transplanted into C 3-rubisco to improve carboxylation rate (V C). Using transplastomic tobacco lines expressing native and mutated rubisco large subunits (L-subunits) from Flaveria pringlei (C 3), Flaveria floridana (C 3-C 4), and Flaveria bidentis (C 4), we reveal that Met-309-Ile substitutions in the L-subunit act as a catalytic switch between C 4 ( 309Ile; faster V C, lower CO 2 affinity) and C 3 ( 309Met; slower VC, higher CO 2 affinity) catalysis. Application of this transplastomic system permits further identification of other structural solutions selected by nature that can increase rubisco V C in C 3 crops. Coengineering a catalytically faster C 3 rubisco and a CO 2-concentrating mechanism within C 3 crop species could enhance their efficiency in resource use and yield.

KW - Chloroplast transformation

KW - CO assimilation

KW - Gas exchange

KW - rbcL mutagenesis

UR - http://www.scopus.com/inward/record.url?scp=80052276565&partnerID=8YFLogxK

U2 - 10.1073/pnas.1109503108

DO - 10.1073/pnas.1109503108

M3 - Journal article

C2 - 21849620

AN - SCOPUS:80052276565

VL - 108

SP - 14688

EP - 14693

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 35

ER -