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PubMed2004

A salinity-induced C3-CAM transition increases energy conservation in the halophyte Mesembryanthemum crystallinum L.

A strongly increased ATP/ADP ratio was found during the nocturnal phase I in crassulacean acid metabolism (CAM)-induced Mesembryanthemum crystallinum plants. Conversely, during the daytime phase III in CAM-performing plants the ATP/ADP ratio dropped to a similar level to that of C3 plants, cytochrome c oxidase activity was stimulated and mitochondrial Mn-superoxide dismutase activity was strongly increased. The findings suggest that a salinity-induced C3-CAM transition might be an efficient energy-conserving strategy for M. crystallinum plants, in which the strong nocturnal ATP production seems to be, at least partially, independent from the coupled mitochondrial electron transport.

Adenosine Diphosphate↗

PubMed1999

Catalase activity during C3-CAM transition in Mesembryanthemum crystallinum L. leaves.

Treatment with 0.4 mol dm(-3) NaCl caused a C3-CAM shift in Mesembryanthemum crystallinum L. leaves. In parallel to the CAM induction the activity of CAT was significantly decreased. In C3 and in CAM plants CAT activity showed daily fluctuations, with the maximum at the end of the light period. The oscillations of CAT were more pronounced in CAM than in C3 plants. In M. crystallinum CAT activity seems to respond more to CAM induction than to salinity.

Catalase↗

PubMed2025

Unraveling the molecular choreography of C3 to CAM transition in Mesembryanthemum crystallinum using phosphoproteomics.

Climate change and population growth threaten global freshwater resources and food security. Crassulacean acid metabolism (CAM) is a specialized photosynthetic adaptation that exhibits superior water use efficiency (WUE) compared to C3 and C4 photosynthesis. Mesembryanthemum crystallinum (common ice plant) is capable of shifting from C3 to CAM, making it a key model for investigating photosynthesis plasticity and its potential to enhance crop stress resilience. To date, the molecular mechanisms underlying this high-WUE photosynthetic transition remain largely unknown. Using mass spectrometry-based proteomics and phosphoproteomics, we quantified 4233 phosphopeptides containing 4758 phosphorylation sites, including the well-characterized Serine 11 of phosphoenolpyruvate carboxylase 1 (PEPC1). It is a critical phosphorylation site facilitating nocturnal CO2 fixation during CAM. Our analysis revealed many phosphorylation sites that exhibited similar diel patterns as the PEPC1 pS11, and they may be part of the regulatory network involved in CAM induction. Glycolysis/gluconeogenesis and carbon storage/breakdown modules exhibited extensive phosphorylation regulation, and vesicle trafficking could play a role in nocturnal carbon fixation. Furthermore, glycine-rich RNA-binding protein 7 (GRP7) in association with cold shock protein 1 (CSP1) emerged as a potential transcriptional switch for nocturnal stomatal opening. On the other hand, ABI5-binding protein 1 (AFP1) and oxidative stress 3 (OXS3)-activated ABA signaling, along with high CO2 signaling and suppressed blue light signaling, may contribute to diurnal stomatal closure. These findings shed light on the protein phosphorylation changes and provide valuable targets for functional characterization of their roles in CAM induction.

Mesembryanthemum↗

PubMed1990

Increased expression of a gene coding for NAD:glyceraldehyde-3-phosphate dehydrogenase during the transition from C3 photosynthesis to crassulacean acid metabolism in Mesembryanthemum crystallinum.

We utilized differential plaque hybridization to identify three cDNA clones for transcripts which increase in abundance during the salinity-induced transition from C3 photosynthesis to crassulacean acid metabolism (CAM) in Mesembryanthemum crystallinum. Although there are differences in the abundance of these transcripts in unstressed tissue, steady-state levels of all three increased within 30 h following irrigation with 0.5 M NaCl. One cDNA encodes the cytosolic form of glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating) (NAD-GAPDH], an enzyme involved in the production of phosphoenolpyruvate for CO2 fixation at night and the conversion of pyruvate to storage carbohydrate during the day. Coding region and 3'-noncoding sequence probes were used to examine the expression of NAD-GAPDH transcripts in leaf and root tissue. We show that the gene encoding the NAD-GAPDH cDNA is expressed in both leaf and root tissue during C3 photosynthesis and CAM. NAD-GAPDH transcript levels increase rapidly in leaf (but not in root) tissue during the transition to CAM. Our data indicate that the predominant NAD-GAPDH transcript expressed during C3 photosynthesis and CAM is encoded by a single gene in M crystallinum. These results imply that the transition to CAM in some cases involves an upward readjustment in the level of a gene product expressed during C3 photosynthesis, rather than the expression of a CAM-specific isoform with unique regulatory or kinetic properties.

Amino Acid Sequence↗

PubMed2006

Phosphoenolpyruvate carboxylase genes in C3, crassulacean acid metabolism (CAM) and C3/CAM intermediate species of the genus Clusia: rapid reversible C3/CAM switches are based on the C3 housekeeping gene.

The genus Clusia includes species that exhibit either the C3 or crassulacean acid metabolism (CAM) mode of photosynthesis, or those that are able to switch between both modes according to water availability. In order to screen for species-specific genetic variability, we investigated the key carboxylase for CAM, phosphoenolpyruvate carboxylase (PEPC). Sequence analysis of DNA isolated from the obligate CAM species, Clusia hilariana, the obligate C3 species, Clusia multiflora, and an intermediate species that can switch between C3 and CAM photosynthesis, Clusia minor, revealed three different isoforms for C. hilariana and one each for the other two species. Sequence alignments indicated that PEPC from the intermediate species had high homology with the C3 protein and with one of CAM plant proteins. These were assumed to constitute 'housekeeping' proteins, which can also support CAM in intermediate species. The other two isoforms of the CAM plant C. hilariana were either CAM-specific or showed homologies with PEPC from roots. Phylogenetic trees derived from neighbour-joining analysis of amino acid sequences from 13 different Clusia species resulted in two distinct groups of plants with either 'housekeeping' PEPC only, or additionally CAM-related isoforms. Only C. hilariana showed the third, probably root-specific isoform. The high homology of the PEPC from the intermediate species with the C3 protein indicates that for the reversible transition from the C3 to CAM mode of photosynthesis, the C3 type of PEPC is sufficient. Its expression, however, is strongly increased under CAM-inducing conditions. The use of the C3 isoform could have facilitated the evolution of CAM within the genus, which occurred independently for several times.

Amino Acid Sequence↗

PubMed1993

Development and Environmental Stress Employ Different Mechanisms in the Expression of a Plant Gene Family.

Ribulose bisphosphate carboxylase small subunit (RbcS) genes in the common ice plant, as in all higher plants, constitute a multigene family. We have measured transcription activity and steady state mRNA levels of individual members of the family, six RbcS genes, in the ice plant with emphasis on the transition from C3 photosynthesis to Crassulacean acid metabolism (CAM), which this plant undergoes during development and under environmental stress. Four RbcS genes are differentially expressed in leaves but are regulated in a coordinate fashion. A developmentally engrained, sharp decline in the steady state mRNA levels, which is observed during the juvenile-to-adult growth phase transition, coincides with the time interval when the C3-to-CAM switch occurs. Developmental down regulation of RbcS is due to down regulation of transcription. In contrast, NaCl stress specifically affected RbcS transcript accumulation post-transcriptionally, resulting in decreased RbcS mRNA levels. Antagonistic regulatory programs are apparent in stress/stress relief experiments. The results indicate complex controls, affecting both transcriptional and post-transcriptional processes, that act differentially during plant development, stress, and recovery from stress.

Journal Article↗

PubMed1995

Age-dependent induction of pyruvate, orthophosphate dikinase in Mesembryanthemum crystallinum L.

A full-length transcript for pyruvate, orthophosphate dikinase (PPDK; EC 2.7.9.1), has been characterized from Mesembryanthemum crystallinum. Under salt stress or with increasing age, this plant shows a transition from C3 to Crassulacean acid metabolism (CAM). The PPDK plays a central role in gluconeogenesis during the light phase of CAM. The transcript is 3165 bases in length with a single open reading frame of 2739 nucleotides specifying a protein of molecular mass 103098, including a transit peptide of mass 7902 for chloroplast import. The protein shares 44-77% sequence identity with PPDK from C4-plants and microorganisms. Known functional and regulatory amino acids are conserved. Southern-type hybridizations indicated one copy or very few closely related copies of the gene per haploid genome. We investigated the induction of PPDK at the mRNA and protein levels, using the well characterized induction of a CAM-form of phosphoenol pyruvate carboxylase (PEPCase) as internal standard. During wilting of excised leaves PEPCase mRNA amounts increased strongly within 8 h. Under these conditions amounts of PPDK mRNA remained constant. Re-hydrating leaves from previously stressed plants led to a decrease in PEPCase and PPDK mRNA amounts. During salt stress, no correlation between PEPCase and PPDK was observed. Analysis of plants of different ages indicated that, even in well-watered plants, PPDK-specific protein and mRNA increased when the plants reached a certain age. In old plants, salt stress failed to further increase PPDK mRNA or protein levels.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1988

Ca2+/calmodulin-dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains.

Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II) autophosphorylated under limiting conditions (7 microM [gamma-32P]ATP, 500 microM magnesium acetate, 4 degrees C) was analyzed by CNBr cleavage and peptide mapping to determine the site of autophosphorylation that brings about transition of the kinase to the Ca2+-independent form. Reverse phase high performance liquid chromatography (HPLC) (C3) revealed one major CN-Br 32P-peptide (CB1) that eluted at about 6% propanol. This peptide contained [32P]threonine, but almost no [32P]serine, and migrated as a single band (Mr = 3000-3500) in polyacrylamide gels run in the presence of urea and sodium dodecyl sulfate. The properties of CB1 were compared to the properties of a 26-residue synthetic peptide containing the CaM-binding and inhibitory domains as well as a consensus phosphorylation sequence (-Arg-Gln-Glu-Thr-) of rat brain CaM-kinase II (residues 282-307 and 283-308 of the alpha and beta subunits, respectively). CB1 and the synthetic peptide comigrated in urea/sodium dodecyl sulfate gels, co-eluted from reverse phase HPLC (C3 and C18) and from Sephadex G-50, and exhibited Ca2+-dependent calmodulin-binding properties. When the two peptides were subjected to automated Edman sequence analysis, both exhibited a burst of 32P release at cycle 5, which is consistent with the expected amino-terminal sequence of the two peptides, i.e. His-Arg-Gln-Glu-Thr(PO4)-. These findings indicate that autophosphorylation of Thr286 (alpha subunit) and Thr287 (beta subunit) is responsible for transition of CaM-kinase II to the Ca2+-independent form.

Adenosine Triphosphate↗

PubMed1992

Polarized rat uterine epithelium in vitro: responses to estrogen in defined medium.

Previously described procedures for the culture of immature rat uterine epithelium (UE) allowed the cells to proliferate to confluence and develop morphological and functional polarity. The present study describes the transition from culture of UE cells in serum to a serum-free defined medium. This was accomplished with no significant alteration in the ability of UE cells to attain morphological and functional polarity. In defined medium, which contained estrogen (2.5 x 10(-9) M), UE cells proliferated to confluence, demonstrated separation of apical and basal plasma membrane domains, and displayed preferential secretion of proteins and proteoglycans from the apical surface. Apical secretions of polarized cultures contained complement component C3, the secreted portion of the immunoglobulin A receptor and the secretory glycoprotein, USP-1. The cell surface adhesion molecule, CAM 105, could be demonstrated at the apical cell surface. Expression of this profile of secretory and cell surface markers, representative of the in vivo estrogen response of immature rat UE cells, correlated with an in vitro state of non-receptivity of polarized UE cells toward blastocysts which remained viable and competent to attach. We conclude that the polarized UE cell that develops in the described defined medium expresses a phenotype similar to that which characterizes the in vivo uterine estrogen response.

Animals↗