Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Manipulation of Rubisco
T2 - the amount, activity, function and regulation
AU - Parry, M. A J
AU - Andralojc, P. J.
AU - Mitchell, R. A C
AU - Madgwick, P. J.
AU - Keys, A. J.
PY - 2003/5/1
Y1 - 2003/5/1
N2 - Genetic modification to increase the specificity of Rubisco for CO2 relative to O2 and to increase the catalytic rate of Rubisco in crop plants would have great agronomic importance. The availability of three-dimensional structures of Rubisco at atomic resolution and the characterization of site-directed mutants have greatly enhanced the understanding of the catalytic mechanism of Rubisco. Considerable progress has been made in identifying natural variation in the catalytic properties of Rubisco from different species and in developing the tools for introducing both novel and foreign Rubisco genes into plants. The additional complexities of assembling copies of the two distinct polypeptide subunits of Rubisco into a functional holoenzyme in vivo (requiring sufficient expression, post-translational modification, interaction with chaperonins, and interaction with Rubisco activase) remain a major challenge. The consequences of changing the amount of Rubisco present in leaves have been investigated by the use of antisense constructs. The manipulation of genes encoding Rubisco activase has provided a means to investigate the regulation of Rubisco activity.
AB - Genetic modification to increase the specificity of Rubisco for CO2 relative to O2 and to increase the catalytic rate of Rubisco in crop plants would have great agronomic importance. The availability of three-dimensional structures of Rubisco at atomic resolution and the characterization of site-directed mutants have greatly enhanced the understanding of the catalytic mechanism of Rubisco. Considerable progress has been made in identifying natural variation in the catalytic properties of Rubisco from different species and in developing the tools for introducing both novel and foreign Rubisco genes into plants. The additional complexities of assembling copies of the two distinct polypeptide subunits of Rubisco into a functional holoenzyme in vivo (requiring sufficient expression, post-translational modification, interaction with chaperonins, and interaction with Rubisco activase) remain a major challenge. The consequences of changing the amount of Rubisco present in leaves have been investigated by the use of antisense constructs. The manipulation of genes encoding Rubisco activase has provided a means to investigate the regulation of Rubisco activity.
KW - Photosynthesis
KW - RbcL rbcS
KW - Rubisco
KW - Specificity factor
KW - Transgenic
UR - http://www.scopus.com/inward/record.url?scp=0037725392&partnerID=8YFLogxK
U2 - 10.1093/jxb/erg141
DO - 10.1093/jxb/erg141
M3 - Journal article
C2 - 12709478
AN - SCOPUS:0037725392
VL - 54
SP - 1321
EP - 1333
JO - Journal of Experimental Botany
JF - Journal of Experimental Botany
SN - 0022-0957
IS - 386
ER -