The life of ribulose 1,5-bisphosphate carboxylase/oxygenase—posttranslational facts and mysteries

Houtz, Robert L.; Portis, Archie R.

doi:10.1016/s0003-9861(03)00122-x

Cited by 85 publications

(51 citation statements)

References 151 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There are three different forms of Rubisco large subunit that showed increased levels by UV-B radiation, whereas two other isoforms are decreased (Table II), and the decrease is in agreement with the previous microarray studies (21). Rubisco large subunit is encoded in the chloroplast and is a unique gene (29); however, it is subject to diverse co-and post-translational modifications, including the acetylation of Pro-3, N-formylation, trimethylation in the ⑀-amino of Lys-14, and carbamylation in the active site; several amino acid modifications occur in some species but not others (30). Thus, even if Rubisco large subunit transcription is down-regulated by UV-B radiation, translational and posttranslational regulation probably occurs to the existing protein.…”

Section: Discussionsupporting

confidence: 89%

Analysis of Leaf Proteome after UV-B Irradiation in Maize Lines Differing in Sensitivity

Casati

Zhang

Burlingame

et al. 2005

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

Section: Discussionsupporting

confidence: 89%

Analysis of Leaf Proteome after UV-B Irradiation in Maize Lines Differing in Sensitivity

Casati

Zhang

Burlingame

et al. 2005

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…Likewise, SSU is also associated with the chloroplast chaperones after cleavage of a transit peptide (Gutteridge and Gatenby 1995). These chaperones promote protein folding of each subunit and assembly of RuBisCO's LSUs and SSUs (Houtz and Portis 2003). LSU is assembled with SSU after dissociation from the chaperone complex to construct a holoenzyme, but the process remains to be revealed in higher plants.…”

Section: Folding and Assembly Into The Rubisco Holoenzyme In Chloroplmentioning

confidence: 99%

“…It was proposed that a bacterial-type chaperone system was involved in the process of folding and assembly into LSU 8 SSU 8 (Brutnell et al 1999;Jarvis and Soll 2001;Houtz and Portis 2003;Kessler and Schnell 2006). Indeed, homologs of DnaJ/DnaK/GrpE possess putative chloroplast-targeted sequences (Wang et al 1993;Brutnell et al 1999).…”

Section: Folding and Assembly Into The Rubisco Holoenzyme In Chloroplmentioning

confidence: 99%

“…Interestingly, they are also present as large protein families in higher plants, 5 CYPs and 11 FKBPs are located in the chloroplast lumen (He et al 2004;Romano et al 2004). In Arabidopsis, it is suggested that CYP38 is involved in the assembly of photosystem II (PSII) and FKBP20-2 is an essential factor for maintenance of the PSII complex (He et al 2007;Lima et al 2007), suggesting the possibility that one or several immunophilins may also be required for RuBisCO assembly (Houtz and Portis 2003). Indeed, several immunophilin proteins are observed or predicted to be in the chloroplast stroma (He et al 2004).…”

Section: Folding and Assembly Into The Rubisco Holoenzyme In Chloroplmentioning

confidence: 99%

See 1 more Smart Citation

Molecular mechanisms of RuBisCO biosynthesis in higher plants

Nishimura

Ogawa

Ashida

et al. 2008

Plant Biotechnology

View full text Add to dashboard Cite

RuBisCO is a key enzyme catalyzing the CO 2 -fixing reaction in the initial step of the Calvin cycle. However, its enzymatic properties are inadequate for plants because of its small turnover rate of the carboxylase reaction (Harris and Koniger 1997) and its low affinity for CO 2 . Thus, this enzyme limits the rate of carbon assimilation and net photosynthesis (Yokota and Shigeoka 2007). To compensate for its enzymatic inefficiencies, RuBisCO comprises as much as half of leaf total soluble proteins in higher plants, corresponding to 30% of total nitrogen compounds in the leaves. Consequently RuBisCO is regarded as the most abundant protein in the world (Gatenby and Ellis 1990;Makino et al. 2003). Indeed, a decrease in the amount of RuBisCO causes strong inhibition of CO 2 assimilation and subsequent growth retardation (Rodermel et al. 1988;Quick et al. 1991;Hudson et al. 1992;Masle et al. 1993). Therefore, it is important to understand how plants synthesize RuBisCO abundantly and maintain a sufficient amount for growth and development. How is RuBisCO synthesized optimally in plant chloroplasts? Gene expression of nuclear-and chloroplast-encoded subunits of RuBisCORuBisCO functions as an enzyme in the chloroplast stroma with a hexadecameric structure consisting of eight large (LSU) and eight small subunits (SSU). LSUs and SSUs are synthesized through distinct processes as the genes encoding them are individually located on different genomes (Figure 1). SSU is encoded by rbcS in the nuclear genome as a multigene family ranging from 2 to 12 members (Gutteridge and Gatenby 1995). The expression of rbcS is regulated by various endogenous and/or exogenous signals, such as light/dark transition, light quality, circadian rhythm, temperature, atmospheric CO 2 concentration, and nitrogen supply. It is also controlled in an organ-and tissue-specific manner, and by developmental stages (Sugita and Gruissem 1987; Dedondar et al. 1993; Pilgrim and McClung 1993;Gesch et al. 1998;Yoon et al. 2001;Imai et al. 2007). The relationship between rbcS expression and light conditions has been studied well. The signal transduction pathway mediated by phytochrome and the G protein is involved in light-stimulated transcription and light quality-dependent expression pattern of rbcS (Zhou 1999). Dark-induced down-regulation of rbcS expression is regulated by CONSTITUTIVELY MORPHOGENIC/ DE-ETHIOLATED/FUSCA (COP/DET/FUS), which are well known as repressors of photomorphogenesis (Millar et al. 1994). However, cis elements or trans-acting factors involved in the regulation of the rbcS expression response to various endogenous and/or exogenous signals are not well understood.After transcription in the nucleus, rbcS mRNA is translated on 80S ribosomes in the cytosol to synthesize the precursor protein of SSU (PreSSU) with the transit peptide in its N-terminal required for targeting to the chloroplast. The PreSSU is carried to the chloroplast outer membrane by heat shock protein70 (hsp70) and 14- Molecular mechanisms of RuBisCO biosynthesis in hi...

show abstract

“…The SET domain methyltransferases differ from other methyltransferases with known structures in that its catalytic core forms a knot-like structure with a conserved tyrosine residue in the active site necessary for catalysis (6 -12). SET domain methyltransferases have been shown to modify a variety of proteins including Rubisco 3 (13,14), cytochrome c (15), and most notably histones (16). Currently, no physiological effect has been observed for the lysine methylation of Rubisco or cytochrome c (14,15).…”

mentioning

confidence: 99%

Yeast Ribosomal/Cytochrome c SET Domain Methyltransferase Subfamily

Porras-Yakushi¹,

Whitelegge²,

Clarke³

2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

Ribosomal protein L23ab is specifically dimethylated at two distinct sites by the SET domain-containing enzyme Rkm1 in the yeast Saccharomyces cerevisiae. Using liquid column chromatography with electrospray-ionization mass spectrometry, we determined that Rpl23ab purified from the ⌬rkm1 deletion strain demonstrated a loss in mass of ϳ56 Da when compared with Rpl23ab purified from the wild type strain. When Rpl23ab was proteolyzed, using proteinase ArgC or CNBr, and the peptides derived were analyzed by tandem mass spectrometry, no sites of methylation were found in Rpl23ab purified from the ⌬rkm1 deletion strain, whereas two sites of dimethylation were observed in the wild type strain at lysine residues 105 and 109. We show that both Rpl23a and Rpl23b are expressed and methylated in vivo in yeast. Using polysomal fractionation, we demonstrate that the deletion of RKM1 has no effect on ribosomal complex formation. Comparison of SET domain methyltransferase substrates in yeast reveal sequence similarities around the lysine methylation sites and suggest that an (Asn/Pro)-Pro-Lys consensus sequence may be a target for methylation by subfamily 2 SET domain methyltransferases. Finally, we show the presence of Rkm1 homologs in fungi, plants, and mammals including humans.SET domain methyltransferases are a new family of methyltransferases known to specifically methylate lysine residues in a variety of proteins (1, 2). The family was named after the Drosophila genes in which it was first discovered, Su(var), Enhancer of zeste, and Trithorax (3), all of which were later shown to encode histone lysine methyltransferases (4 -6). The SET domain methyltransferases differ from other methyltransferases with known structures in that its catalytic core forms a knot-like structure with a conserved tyrosine residue in the active site necessary for catalysis (6 -12). SET domain methyltransferases have been shown to modify a variety of proteins including Rubisco 3 (13, 14), cytochrome c (15), and most notably histones (16). Currently, no physiological effect has been observed for the lysine methylation of Rubisco or cytochrome c (14, 15). However, in histones lysine methylation has been shown to play an important role in the activation or repression of transcription through modulating the structure of chromatin (16).Histone tails are highly decorated by lysine methylation reactions and the majority of these modifications occur in close proximity and can exhibit opposite effects. The most well characterized biology involves the interplay between the methylation of lysine 4 and lysine 9 of mammalian histone H3, catalyzed by distinct SET domain methyltransferases (16). Methylation of lysine 4 is correlated with active transcription and euchromatin, whereas methylation of lysine 9 is associated with repressed transcription and heterochromatin (17)(18)(19)(20). In yeast, histone H3 methylation has also been actively studied and a similar interplay has been observed, although the distance between the methylated sites is greater. Histone H...

show abstract

The life of ribulose 1,5-bisphosphate carboxylase/oxygenase—posttranslational facts and mysteries

Cited by 85 publications

References 151 publications

Analysis of Leaf Proteome after UV-B Irradiation in Maize Lines Differing in Sensitivity

Analysis of Leaf Proteome after UV-B Irradiation in Maize Lines Differing in Sensitivity

Molecular mechanisms of RuBisCO biosynthesis in higher plants

Yeast Ribosomal/Cytochrome c SET Domain Methyltransferase Subfamily

Contact Info

Product

Resources

About