Abstract
Electron impact mass spectronomy analysis of the amino‐terminal amino acid of the small subunit (SSU) of ribulose‐1,5‐bisphosphate carboxylase (Rubisco) showed that the amino‐terminal methionine residue is post‐translationally modified to N‐methyl‐methionine. Modification of the amino‐terminal methionine residue was found in mature SSU proteins from the dicotyledonous plants pea and spinach as well as the monocotyledonous plants barley and corn. SSU methyltransferase is a soluble protein in the chloroplast stroma and accepts heterologously expressed non‐methylated SSU as a substrate using S‐adenosylmethionine as methyl‐group donor. We show that this modification occurs after post‐translational uptake of the precursor form of SSU into chloroplasts and processing to its mature size. This reaction represents a new step in the import and assembly pathway of Rubisco holoenzyme.
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Dates
Type | When |
---|---|
Created | 22 years, 10 months ago (Oct. 11, 2002, 6:59 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 11:19 a.m.) |
Indexed | 4 weeks ago (Aug. 6, 2025, 9:55 a.m.) |
Issued | 28 years, 3 months ago (May 26, 1997) |
Published | 28 years, 3 months ago (May 26, 1997) |
Published Online | 27 years, 10 months ago (Oct. 28, 1997) |
Published Print | 28 years, 3 months ago (May 26, 1997) |
@article{Grimm_1997, title={Postimport methylation of the small subunit of ribulose‐1,5‐bisphosphate carboxylase in chloroplasts}, volume={408}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(97)00462-6}, DOI={10.1016/s0014-5793(97)00462-6}, number={3}, journal={FEBS Letters}, publisher={Wiley}, author={Grimm, Rudolf and Grimm, Monika and Eckerskorn, Christoph and Pohlmeyer, Kai and Röhl, Thomas and Soll, Jürgen}, year={1997}, month=may, pages={350–354} }