Characterization of Chloroplastic Fructose 1,6-Bisphosphate Aldolases as Lysine-methylated Proteins in Plants

Mininno, Morgane; Brugière, Sabine; Pautre, Virginie; Gilgen, Annabelle; Ma, Shuang‐Gang; Ferro, Myriam; Tardif, Marianne; Alban, Claude; Ravanel, Stéphane

doi:10.1074/jbc.m112.359976

Cited by 57 publications

(86 citation statements)

References 36 publications

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“…Acetylation and methylation of chloroplast proteins have been identified recently (Houtz et al, 1992;Finkemeier et al, 2011;Wu et al, 2011;Mininno et al, 2012;Alban et al, 2014). Therefore, the acetylation and methylation states of the four membrane-bound AtFNR forms were analyzed.…”

Section: Atfnr1 and Atfnr2 Are Lys Acetylatedmentioning

confidence: 99%

Posttranslational Modifications of FERREDOXIN-NADP+ OXIDOREDUCTASE in Arabidopsis Chloroplasts

et al. 2014

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Rapid responses of chloroplast metabolism and adjustments to photosynthetic machinery are of utmost importance for plants' survival in a fluctuating environment. These changes may be achieved through posttranslational modifications of proteins, which are known to affect the activity, interactions, and localization of proteins. Recent studies have accumulated evidence about the crucial role of a multitude of modifications, including acetylation, methylation, and glycosylation, in the regulation of chloroplast proteins. Both of the Arabidopsis (Arabidopsis thaliana) leaf-type FERREDOXIN-NADP + OXIDOREDUCTASE (FNR) isoforms, the key enzymes linking the light reactions of photosynthesis to carbon assimilation, exist as two distinct forms with different isoelectric points. We show that both AtFNR isoforms contain multiple alternative amino termini and undergo lightresponsive addition of an acetyl group to the a-amino group of the amino-terminal amino acid of proteins, which causes the change in isoelectric point. Both isoforms were also found to contain acetylation of a conserved lysine residue near the active site, while no evidence for in vivo phosphorylation or glycosylation was detected. The dynamic, multilayer regulation of AtFNR exemplifies the complex regulatory network systems controlling chloroplast proteins by a range of posttranslational modifications, which continues to emerge as a novel area within photosynthesis research.

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Section: Atfnr1 and Atfnr2 Are Lys Acetylatedmentioning

confidence: 99%

Posttranslational Modifications of FERREDOXIN-NADP+ OXIDOREDUCTASE in Arabidopsis Chloroplasts

et al. 2014

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“…Moreover, three isoforms of chloroplast FRU-1,6-BISPHOSPHATE ALDOLASE have been found to contain trimethylated Lys residues in close proximity to their C termini. No differences, however, could be detected in the catalytic activity, stability, or oligomerization between the trimethylated and unmodified enzymes (Mininno et al, 2012).…”

Section: Lys and Arg Methylationmentioning

confidence: 84%

“…A recent study has identified 23 chloroplast methylproteins (Alban et al, 2014), including the previously described ALDOLASE isoforms (Mininno et al, 2012) and PLASTID RIBOSOMAL PROTEIN L11 (Yamaguchi and Subramanian, 2000). Four out of these 23 proteins contained one or more methylated Arg residues, while 17 proteins had Lys methylation.…”

Section: Lys and Arg Methylationmentioning

confidence: 97%

“…RLSMT was shown to exist in complex with Rubisco (Raunser et al, 2009) in which the Lys-14 is trimethylated in several species belonging to the Fabaceae, Solanaceae, and Cucurbitaceae families but not in wheat (Triticum aestivum), spinach (Spinacia oleracea), or Arabidopsis (Houtz et al, 1992;Mininno et al, 2012). Despite numerous studies, the effects of Lys-14 trimethylation of RBCL have not been defined, and RLSMT knockdown plants do not show marked defects in growth and CO 2 assimilation (Mininno et al, 2012). Moreover, three isoforms of chloroplast FRU-1,6-BISPHOSPHATE ALDOLASE have been found to contain trimethylated Lys residues in close proximity to their C termini.…”

Section: Lys and Arg Methylationmentioning

confidence: 99%

“…Moreover, it is notable that a specific Lys residue may be targeted for either acetylation or methylation, and thus these modifications may have either antagonistic or cooperative effects in vivo (Rice and Allis, 2001), not to mention various other types of possible modifications. Hence, the recently identified acetylation of Lys-14 in Arabidopsis RBCL (Finkemeier et al, 2011) may prevent the well-documented interaction of RLSMT with Rubisco in a catalytically productive way (Mininno et al, 2012).…”

Section: Lys and Arg Methylationmentioning

confidence: 99%

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Posttranslational Modifications of Chloroplast Proteins: An Emerging Field

2015

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Posttranslational modifications of proteins are key effectors of enzyme activity, protein interactions, targeting, and turnover rate, but despite their importance, they are still poorly understood in plants. Although numerous reports have revealed the regulatory role of protein phosphorylation in photosynthesis, various other protein modifications have been identified in chloroplasts only recently. It is known that posttranslational N a -acetylation occurs in both nuclear-and plastid-encoded chloroplast proteins, but the physiological significance of this acetylation is not yet understood. Lysine acetylation affects the localization and activity of key metabolic enzymes, and it may work antagonistically or cooperatively with lysine methylation, which also occurs in chloroplasts. In addition, tyrosine nitration may help regulate the repair cycle of photosystem II, while N-glycosylation determines enzyme activity of chloroplastic carbonic anhydrase. This review summarizes the progress in the research field of posttranslational modifications of chloroplast proteins and points out the importance of these modifications in the regulation of chloroplast metabolism.

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The functional diversity of protein lysine methylation

Lanouette

Mongeon

Figeys

et al. 2014

Molecular Systems Biology

223

213

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Large-scale characterization of post-translational modifications (PTMs), such as phosphorylation, acetylation and ubiquitination, has highlighted their importance in the regulation of a myriad of signaling events. While high-throughput technologies have tremendously helped cataloguing the proteins modified by these PTMs, the identification of lysine-methylated proteins, a PTM involving the transfer of one, two or three methyl groups to the e-amine of a lysine side chain, has lagged behind. While the initial findings were focused on the methylation of histone proteins, several studies have recently identified novel non-histone lysinemethylated proteins. This review provides a compilation of all lysine methylation sites reported to date. We also present key examples showing the impact of lysine methylation and discuss the circuitries wired by this important PTM.

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Characterization of Chloroplastic Fructose 1,6-Bisphosphate Aldolases as Lysine-methylated Proteins in Plants

Cited by 57 publications

References 36 publications

Posttranslational Modifications of FERREDOXIN-NADP+ OXIDOREDUCTASE in Arabidopsis Chloroplasts

Posttranslational Modifications of FERREDOXIN-NADP+ OXIDOREDUCTASE in Arabidopsis Chloroplasts

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field

The functional diversity of protein lysine methylation

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