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Rubisco activase activity assays

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Rubisco activase activity assays. / Barta, Csengele; Carmo-Silva, A. Elizabete; Salvucci, Michael E.
In: Methods in Molecular Biology, Vol. 684, 07.03.2011, p. 375-382.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Barta, C, Carmo-Silva, AE & Salvucci, ME 2011, 'Rubisco activase activity assays', Methods in Molecular Biology, vol. 684, pp. 375-382. https://doi.org/10.1007/978-1-60761-925-3_29

APA

Barta, C., Carmo-Silva, A. E., & Salvucci, M. E. (2011). Rubisco activase activity assays. Methods in Molecular Biology, 684, 375-382. https://doi.org/10.1007/978-1-60761-925-3_29

Vancouver

Barta C, Carmo-Silva AE, Salvucci ME. Rubisco activase activity assays. Methods in Molecular Biology. 2011 Mar 7;684:375-382. doi: 10.1007/978-1-60761-925-3_29

Author

Barta, Csengele ; Carmo-Silva, A. Elizabete ; Salvucci, Michael E. / Rubisco activase activity assays. In: Methods in Molecular Biology. 2011 ; Vol. 684. pp. 375-382.

Bibtex

@article{10218cf5dcf042b5ac672db90b13bd01,
title = "Rubisco activase activity assays",
abstract = "Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) activase functions as a mechano-chemical motor protein using the energy from ATP hydrolysis to contort the structure of its target protein, Rubisco. This action modulates the activation state of Rubisco by removing tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites, thereby restoring the sites to catalytic competence. This chapter reports methods developed for assaying the two activities of Rubisco activase: ATP hydrolysis and Rubisco activation.",
keywords = "AAA+ protein, ATP hydrolysis, Calvin Cycle, CO2 fixation, Rubisco activase, Rubisco, RuBP ",
author = "Csengele Barta and Carmo-Silva, {A. Elizabete} and Salvucci, {Michael E.}",
year = "2011",
month = mar,
day = "7",
doi = "10.1007/978-1-60761-925-3_29",
language = "English",
volume = "684",
pages = "375--382",
journal = "Methods in Molecular Biology",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - Rubisco activase activity assays

AU - Barta, Csengele

AU - Carmo-Silva, A. Elizabete

AU - Salvucci, Michael E.

PY - 2011/3/7

Y1 - 2011/3/7

N2 - Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) activase functions as a mechano-chemical motor protein using the energy from ATP hydrolysis to contort the structure of its target protein, Rubisco. This action modulates the activation state of Rubisco by removing tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites, thereby restoring the sites to catalytic competence. This chapter reports methods developed for assaying the two activities of Rubisco activase: ATP hydrolysis and Rubisco activation.

AB - Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) activase functions as a mechano-chemical motor protein using the energy from ATP hydrolysis to contort the structure of its target protein, Rubisco. This action modulates the activation state of Rubisco by removing tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites, thereby restoring the sites to catalytic competence. This chapter reports methods developed for assaying the two activities of Rubisco activase: ATP hydrolysis and Rubisco activation.

KW - AAA+ protein

KW - ATP hydrolysis

KW - Calvin Cycle

KW - CO2 fixation

KW - Rubisco activase

KW - Rubisco

KW - RuBP

U2 - 10.1007/978-1-60761-925-3_29

DO - 10.1007/978-1-60761-925-3_29

M3 - Journal article

C2 - 20960144

AN - SCOPUS:79952117905

VL - 684

SP - 375

EP - 382

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -