Regular ArticleAffinity Purification of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Large Subunit ϵN-Methyltransferase
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Molecular Evolution of the Substrate Specificity of Chloroplastic Aldolases/Rubisco Lysine Methyltransferases in Plants
2016, Molecular PlantCitation Excerpt :One member of this subclass is located in chloroplasts, and the enzyme from pea (Pisum sativum) was originally shown to trimethylate Lys14 of the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme that catalyzes the CO2 fixation step during photosynthesis. The enzyme was named PsLSMT for Pisum sativum Large Subunit Rubisco Methyltransferase (Wang et al., 1995). PsLSMT was extensively characterized at the biochemical and structural levels (for reviews, see Dirk et al., 2006; Houtz et al., 2008).
Neuroprotective effects of hypothermia on synaptic actin cytoskeletal changes induced by perinatal asphyxia
2014, Brain ResearchCitation Excerpt :Protein was quantified by Bradford’s method (Bradford 1976) [12] using bovine serum albumin as standard. Western blot analysis was carried out using PSD fractions separated on 10% SDS-PAGE and the transfer of separated proteins to polyvinylidene difluoride (PVDF) membrane were performed as described previously (Wang et al., 1995; Dunah et al., 1996; Luo et al., 1996). Samples containing 20 μg of protein from each groups were applied to each lane.
Polypeptide substrate specificity of PsLSMT: A set domain protein methyltransferase
2007, Journal of Biological ChemistryCitation Excerpt :At least one study, capitalizing on high resolution ternary complexes formed between SET 7/9 and polypeptide substrates, used a consensus recognition sequence to predict other potential polypeptide substrates for SET7/9 and verified the substrate in vitro (18). Although LSMT has provided important structural and molecular information regarding the SET domain and the catalytic mechanism for protein lysyl methylation (20, 21, 35, 43), ternary complexes between LSMT and polypeptide substrates have not proven feasible as with other SET domain PKMTs. Small synthetic polypeptides do not bind with appreciable affinity to LSMT, and co-crystallization with Rubisco has been unsuccessful.
High-performance catalytic chromatography: The adapter approach
2005, Journal of Chromatography AThe life of ribulose 1,5-bisphosphate carboxylase/oxygenase - Posttranslational facts and mysteries
2003, Archives of Biochemistry and Biophysics