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3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine394
3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine394
-
-
-
?
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
S-adenosyl-L-homocysteine + [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine
S-adenosyl-L-homocysteine + [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-N6,N6,N6-trimethyl-L-lysine
-
mutagenesis of lysine residues 8, 18 and 28 to either Arg or Ala does not affect methylation of Lys-14 by the enzyme, whereas mutagenesis of the Lys-14 methylation site abolishes methylation
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-
?
S-adenosyl-L-methionine + [acyl carrier protein I precursor]-L-lysine
S-adenosyl-L-homocysteine + [acyl carrier protein I precursor]-N6,N6,N6-trimethyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine
S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
the substrate is trimethylated at a conserved lysyl residue located close to the C terminus
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-
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + [granule-bound starch synthase I precursor]-L-lysine
S-adenosyl-L-homocysteine + [granule-bound starch synthase I precursor]-N6,N6,N6-trimethyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + [NAD(P)H-quinone oxidoreductase chain 5]-L-lysine
S-adenosyl-L-homocysteine + [NAD(P)H-quinone oxidoreductase chain 5]-N6,N6,N6-trimethyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-N6,N6,N6-trimethyl-L-lysine
-
no natural substrate. The enzyme is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive
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-
?
S-adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
-
-
-
-
?
additional information
?
-
3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
i.e. RBCL
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
additional information
?
-
no trimethylation of the Rubisco large subunit by the enzyme from Arabidosis thaliana
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-
additional information
?
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no trimethylation of the Rubisco large subunit by the enzyme from Arabidosis thaliana
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3 adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
3 S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine
S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
the substrate is trimethylated at a conserved lysyl residue located close to the C terminus
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
-
-
?
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malfunction
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knockdown of the LSMT homologue in transgenic tobacco plants results in a 2fold decrease of alpha-tocopherol
evolution
molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants, overview. The His-Ala/Pro-Trp triad located in the central part of LSMT enzymes is the key motif to confer the capacity to trimethylate Rubisco. Two of the critical residues are located on a surface loop outside the methyltransferase catalytic site. A strict correlation between the presence of the triad motif and the in vivo methylation status of Rubisco is observed, distribution of the motif into a phylogenetic tree, overview. Chloroplastic fructose-1,6-bisphosphate aldolases (FBAs) are naturally trimethylated in both Pisum sativum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former species. The distribution of the motif into a phylogenetic tree further suggests that the ancestral function of LSMT was FBA trimethylation. In a recent event during higher plant evolution, this function evolved in ancestors of Fabaceae, Cucurbitaceae, and Rosaceae to include Rubisco as an additional substrate to the archetypal enzyme
evolution
molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants, overview. The His-Ala/Pro-Trp triad located in the central part of LSMT enzymes is the key motif to confer the capacity to trimethylate Rubisco. Two of the critical residues are located on a surface loop outside the methyltransferase catalytic site. A strict correlation between the presence of the triad motif and the in vivo methylation status of Rubisco is observed, distribution of the motif into a phylogenetic tree, overview. Chloroplastic fructose-1,6-bisphosphate aldolases (FBAs) are naturally trimethylated in both Pisum sativum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former species. The distribution of the motif into a phylogenetic tree further suggests that the ancestral function of LSMT was FBA trimethylation. In a recent event during higher plant evolution, this function evolved in ancestors of Fabaceae, Cucurbitaceae, and Rosaceae to include Rubisco as an additional substrate to the archetypal enzyme
additional information
structure of PsLSMT enzyme in complex with the AdoMet structural analogue aza-adenosyl-Lmethionine (PDB ID 2H2E), overview
additional information
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structure of PsLSMT enzyme in complex with the AdoMet structural analogue aza-adenosyl-Lmethionine (PDB ID 2H2E), overview
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247H/Ins254A/R259W
mutant is able to methylate both Rubisco and fructose 1,6-bisphosphate aldolase with similar efficiency
I242V
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
Ins254A
enzyme is able to methylate Rubisco in addition to fructose 1,6-bisphosphate aldolase
Ins254A/R259W
mutation enhances methylation of Rubisco without altering fructose 1,6-bisphosphate aldolase methylation
P240A
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
R259W
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
S299P
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
V269L
mutant is not able to methylate Rubisco but rather behaves as wild-type LSMT
Y247H
mutant is not able to methylate Rubisco, activity is severely impaired
additional information
construction of chimera between Pisum sativum and Arabidopsis thaliana enzymes to localize regions of the enzymes responsible for the observed difference in substrate specificity. Contrary to the Pisum sativum enzyme, Arabidopsis thaliana LSMT is not able to trimethylate Rubisco
additional information
-
construction of chimera between Pisum sativum and Arabidopsis thaliana enzymes to localize regions of the enzymes responsible for the observed difference in substrate specificity. Contrary to the Pisum sativum enzyme, Arabidopsis thaliana LSMT is not able to trimethylate Rubisco
additional information
identification of an LSMT region important for RBCL methylation by domain swapping, Arabidopsis thaliana AtLSMT and Pisum sativum PsLSMT are selected as representatives of monofunctional and bifunctional enzymes, respectively. An initial set of chimeric enzymes (chimera 1 and 2) is constructed in which the N-terminal portion of one parental mature enzyme, i.e. devoid of its amino terminal sequence for targeting to plastids, is replaced by the equivalent of the second parental enzyme, and vice versa. The exchanged peptide fragment comprises the nSET domain, the N-terminal part of the SET domain, and the entire iSET domain of both model enzymes. Chimera 1, bearing the N-terminal portion from PsLSMT, displays an AtLSMT-like activity, methylating only FBA2, while its reciprocal counterpart, chimera 2, displays a PsLSMT-like profile, methylating both FBA2 and RBCL. For chimera 2, measured activities are somewhat impaired compared with those of the PsLSMT parent enzyme. Chimera 1 and 2 confirm that the iSET domain is not critical for LSMT substrate selectivity. Phenotypes overview
additional information
-
identification of an LSMT region important for RBCL methylation by domain swapping, Arabidopsis thaliana AtLSMT and Pisum sativum PsLSMT are selected as representatives of monofunctional and bifunctional enzymes, respectively. An initial set of chimeric enzymes (chimera 1 and 2) is constructed in which the N-terminal portion of one parental mature enzyme, i.e. devoid of its amino terminal sequence for targeting to plastids, is replaced by the equivalent of the second parental enzyme, and vice versa. The exchanged peptide fragment comprises the nSET domain, the N-terminal part of the SET domain, and the entire iSET domain of both model enzymes. Chimera 1, bearing the N-terminal portion from PsLSMT, displays an AtLSMT-like activity, methylating only FBA2, while its reciprocal counterpart, chimera 2, displays a PsLSMT-like profile, methylating both FBA2 and RBCL. For chimera 2, measured activities are somewhat impaired compared with those of the PsLSMT parent enzyme. Chimera 1 and 2 confirm that the iSET domain is not critical for LSMT substrate selectivity. Phenotypes overview
additional information
construction of chimera between Pisum sativum and Arabidopsis thaliana enzymes to localize regions of the enzymes responsible for the observed difference in substrate specificity. Contrary to the Pisum sativum enzyme, Arabidopsis thaliana LSMT is not able to trimethylate Rubisco
additional information
-
construction of chimera between Pisum sativum and Arabidopsis thaliana enzymes to localize regions of the enzymes responsible for the observed difference in substrate specificity. Contrary to the Pisum sativum enzyme, Arabidopsis thaliana LSMT is not able to trimethylate Rubisco
additional information
identification of an LSMT region important for RBCL methylation by domain swapping, Arabidopsis thaliana AtLSMT and Pisum sativum PsLSMT are selected as representatives of monofunctional and bifunctional enzymes, respectively. An initial set of chimeric enzymes (chimera 1 and 2) is constructed in which the N-terminal portion of one parental mature enzyme, i.e. devoid of its amino terminal sequence for targeting to plastids, is replaced by the equivalent of the second parental enzyme, and vice versa. The exchanged peptide fragment comprises the nSET domain, the N-terminal part of the SET domain, and the entire iSET domain of both model enzymes. Chimera 1, bearing the N-terminal portion from PsLSMT, displays an AtLSMT-like activity, methylating only FBA2, while its reciprocal counterpart, chimera 2, displays a PsLSMT-like profile, methylating both FBA2 and RBCL. For chimera 2, measured activities are somewhat impaired compared with those of the PsLSMT parent enzyme. Chimera 1 and 2 confirm that the iSET domain is not critical for LSMT substrate selectivity. Phenotypes overview
additional information
-
identification of an LSMT region important for RBCL methylation by domain swapping, Arabidopsis thaliana AtLSMT and Pisum sativum PsLSMT are selected as representatives of monofunctional and bifunctional enzymes, respectively. An initial set of chimeric enzymes (chimera 1 and 2) is constructed in which the N-terminal portion of one parental mature enzyme, i.e. devoid of its amino terminal sequence for targeting to plastids, is replaced by the equivalent of the second parental enzyme, and vice versa. The exchanged peptide fragment comprises the nSET domain, the N-terminal part of the SET domain, and the entire iSET domain of both model enzymes. Chimera 1, bearing the N-terminal portion from PsLSMT, displays an AtLSMT-like activity, methylating only FBA2, while its reciprocal counterpart, chimera 2, displays a PsLSMT-like profile, methylating both FBA2 and RBCL. For chimera 2, measured activities are somewhat impaired compared with those of the PsLSMT parent enzyme. Chimera 1 and 2 confirm that the iSET domain is not critical for LSMT substrate selectivity. Phenotypes overview
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Magnani, R.; Nayak, N.R.; Mazarei, M.; Dirk, L.M.; Houtz, R.L.
Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase
J. Biol. Chem.
282
27857-27864
2007
Pisum sativum
brenda
Mininno, M.; Brugiere, S.; Pautre, V.; Gilgen, A.; Ma, S.; Ferro, M.; Tardif, M.; Alban, C.; Ravanel, S.
Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants
J. Biol. Chem.
287
21034-21044
2012
Arabidopsis thaliana
brenda
Ma, S.; Martin-Laffon, J.; Mininno, M.; Gigarel, O.; Brugiere, S.; Bastien, O.; Tardif, M.; Ravanel, S.; Alban, C.
Molecular evolution of the substrate specificity of chloroplastic aldolases/Rubisco lysine methyltransferases in plants
Mol. Plant
9
569-581
2016
Pisum sativum (Q43088), Pisum sativum, Arabidopsis thaliana (Q9XI84), Arabidopsis thaliana
brenda