The genes for CA1Pase (2-carboxy-D-arabinitol-1-bisphosphate phosphatase) from French bean, wheat, Arabidopsis and tobacco were identified and cloned. The deduced protein sequence included an N-terminal motif identical with the PGM (phosphoglycerate mutase) active site sequence [LIVM]-x-R-H-G-[EQ]-x-x-[WN]. The corresponding gene from wheat coded for an enzyme with the properties published for CA1Pase. The expressed protein lacked PGM activity but rapidly dephosphorylated 2,3-DPG (2,3-diphosphoglycerate) to 2-phosphoglycerate. DTT (dithiothreitol) activation and GSSG inactivation of this enzyme was pH-sensitive, the greatest difference being apparent at pH 8. The presence of the expressed protein during in vitro measurement of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) activity prevented a progressive decline in Rubisco turnover. This was due to the removal of an inhibitory bisphosphate that was present in the RuBP (ribulose-1,5-bisphosphate) preparation, and was found to be PDBP (D-glycero-2,3-pentodiulose-1,5-bisphosphate). The substrate specificity of the expressed protein indicates a role for CA1Pase in the removal of ‘misfire’ products of Rubisco.
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Research Article|
February 24 2012
2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation Available to Purchase
Paul John Andralojc;
Paul John Andralojc
1
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
1Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Pippa J. Madgwick;
Pippa J. Madgwick
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
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Yong Tao;
Yong Tao
2
†DuPont Stine-Haskell Research Center, Newark, DE 19714, U.S.A.
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Alfred Keys;
Alfred Keys
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
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Jane L. Ward;
Jane L. Ward
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
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Michael H. Beale;
Michael H. Beale
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
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Jane E. Loveland;
Jane E. Loveland
3
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
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Phil J. Jackson;
Phil J. Jackson
‡Chemical and Process Engineering, University of Sheffield, Sheffield S3 7RD, U.K.
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Antony C. Willis;
Antony C. Willis
§MRC Immunochemistry Unit, University of Oxford, Oxford OX1 3QU, U.K.
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Steven Gutteridge;
Steven Gutteridge
†DuPont Stine-Haskell Research Center, Newark, DE 19714, U.S.A.
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Martin A.J. Parry
Martin A.J. Parry
1
*Department of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, U.K.
1Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Publisher: Portland Press Ltd
Received:
August 05 2011
Revision Received:
November 21 2011
Accepted:
December 02 2011
Accepted Manuscript online:
December 02 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 442 (3): 733–742.
Article history
Received:
August 05 2011
Revision Received:
November 21 2011
Accepted:
December 02 2011
Accepted Manuscript online:
December 02 2011
Citation
Paul John Andralojc, Pippa J. Madgwick, Yong Tao, Alfred Keys, Jane L. Ward, Michael H. Beale, Jane E. Loveland, Phil J. Jackson, Antony C. Willis, Steven Gutteridge, Martin A.J. Parry; 2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation. Biochem J 15 March 2012; 442 (3): 733–742. doi: https://doi.org/10.1042/BJ20111443
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