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@ARTICLE{Chatterjee:904495,
author = {Chatterjee, Jolly and Coe, Robert A and Acebron, Kelvin and
Thakur, Vivek and Yennamalli, Ragothaman M and Danila,
Florence and Lin, Hsiang-Chun and Balahadia, Christian Paolo
and Bagunu, Efren and Padhma, Preiya P O S and Bala, Soumi
and Yin, Xiaojia and Rizal, Govinda and Dionora, Jacqueline
and Furbank, Robert T and von Caemmerer, Susanne and Quick,
William Paul},
title = {{A} low {CO}2-responsive mutant of {S}etaria viridis
reveals that reduced carbonic anhydrase limits {C}4
photosynthesis},
journal = {The journal of experimental botany},
volume = {72},
number = {8},
issn = {0022-0957},
address = {Oxford},
publisher = {Oxford Univ. Press},
reportid = {FZJ-2021-06065},
pages = {3122 - 3136},
year = {2021},
abstract = {In C4 species, β-carbonic anhydrase (CA), localized to the
cytosol of the mesophyll cells, accelerates the
interconversion of CO2 to HCO3–, the substrate used by
phosphoenolpyruvate carboxylase (PEPC) in the first step of
C4 photosynthesis. Here we describe the identification and
characterization of low CO2-responsive mutant 1 (lcr1)
isolated from an N-nitroso-N-methylurea- (NMU) treated
Setaria viridis mutant population. Forward genetic
investigation revealed that the mutated gene Sevir.5G247800
of lcr1 possessed a single nucleotide transition from
cytosine to thymine in a β-CA gene causing an amino acid
change from leucine to phenylalanine. This resulted in
severe reduction in growth and photosynthesis in the mutant.
Both the CO2 compensation point and carbon isotope
discrimination values of the mutant were significantly
increased. Growth of the mutants was stunted when grown
under ambient pCO2 but recovered at elevated pCO2. Further
bioinformatics analyses revealed that the mutation has led
to functional changes in one of the conserved residues of
the protein, situated near the catalytic site. CA transcript
accumulation in the mutant was $80\%$ lower, CA protein
accumulation $30\%$ lower, and CA activity $~98\%$ lower
compared with the wild type. Changes in the abundance of
other primary C4 pathway enzymes were observed; accumulation
of PEPC protein was significantly increased and accumulation
of malate dehydrogenase and malic enzyme decreased. The
reduction of CA protein activity and abundance in lcr1
restricts the supply of bicarbonate to PEPC, limiting C4
photosynthesis and growth. This study establishes
Sevir.5G247800 as the major CA allele in Setaria for C4
photosynthesis and provides important insights into the
function of CA in C4 photosynthesis that would be required
to generate a rice plant with a functional C4 biochemical
pathway.},
cin = {IBG-2},
ddc = {580},
cid = {I:(DE-Juel1)IBG-2-20101118},
pnm = {2171 - Biological and environmental resources for
sustainable use (POF4-217)},
pid = {G:(DE-HGF)POF4-2171},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:33528493},
UT = {WOS:000642310500024},
doi = {10.1093/jxb/erab039},
url = {https://juser.fz-juelich.de/record/904495},
}