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The regulation of the genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase was examined in amaranth cotyledons in response to changes in illumination. When dark-grown cotyledons were transferred into light, synthesis of the large- and small-subunit polypeptides was initiated very rapidly, before any increase in the levels of their corresponding mRNAs. Similarly, when light-grown cotyledons were transferred to total darkness, synthesis of the large- and small-subunit proteins was rapidly depressed without changes in mRNA levels for either subunit. In vitro translation or in vivo pulse-chase experiments indicated that these apparent changes in protein synthesis were not due to alterations in the functionality of the mRNAs or to protein turnover, respectively. These results, in combination with our previous studies, suggest that the expression of ribulose 1,5-bisphosphate carboxylase genes can be adjusted rapidly at the translational level and over a longer period through changes in mRNA accumulation.
Mol Cell Biol 1986 Jul
PMID:Translational regulation of light-induced ribulose 1,5-bisphosphate carboxylase gene expression in amaranth. 378 98

We have sequenced the two genes for the small subunit of ribulose bisphosphate carboxylase/oxygenase (Rubisco) in Chlamydomonas reinhardtii and analyzed their expression. The two genes encode variant small subunits that differ by four amino acid residues. Both genes are expressed and each is transcribed into an RNA of distinct size. The accumulation of the two RNAs changes depending on the growth conditions, so the small subunit composition of Rubisco may be expected to differ in response to the environment. The C. reinhardtii small subunit sequence is homologous to those of vascular plants or cyanobacteria, but is longer at the amino terminus and in internal positions. The number and location of the intervening sequences in the genes from C. reinhardtii and from other plants differ. In several cases, internal length differences in the polypeptide coincide with the positions of introns in the coding sequence. Thus, changes in the exon structure of the genes during evolution may have been accompanied by substantial changes in the encoded protein. The translation and splicing signals in C. reinhardtii are similar to those of other eukaryotes, but the transcription signals are less conserved and the highly biased codon usage is very unusual.
J Mol Biol 1986 Oct 05
PMID:Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. 382 Feb 91

The regulation of expression of the genes encoding the large subunit (LSU) and small subunit (SSU) of ribulose 1,5-bisphosphate carboxylase (RuBPCase) was examined in 1- through 8-day-old, dark-grown (etiolated) and light-grown amaranth cotyledons. RuBPCase specific activity in light-grown cotyledons increased during this 8-day period to a level 15-fold higher than in dark-grown cotyledons. Under both growth conditions, the accumulation of the LSU and SSU polypeptides was not coordinated. Initial detection of the SSU occurred 1 and 2 days after the appearance of the LSU in light- and dark-grown cotyledons, respectively. Furthermore, although the levels of the LSU were similar in both light- and dark-grown seedlings, the amount of the SSU followed clearly the changes in enzyme activity. Synthesis of these two polypeptides was dramatically different in etiolated versus light-grown cotyledons. In light the synthesis of both subunits was first observed on day 2 and continued throughout the growth of the cotyledons. In darkness the rate of synthesis of both subunits was much lower than in light and occurred only as a burst between days 2 and 5 after planting. However, mRNAs for both subunits were present in etiolated cotyledons at similar levels on days 4 through 7 (by Northern analysis) and were functional in vitro, despite their apparent inactivity in vivo after day 5. In addition, since both LSU and SSU mRNA levels were lower in dark- than in light-grown seedlings, our results indicate that both transcriptional and post-transcriptional controls modulate RuBPCase production in developing amaranth cotyledons.
Mol Cell Biol 1985 Sep
PMID:Transcriptional and post-transcriptional regulation of ribulose 1,5-bisphosphate carboxylase gene expression in light- and dark-grown amaranth cotyledons. 383 89

The maize chloroplast gene coding for the large subunit of ribulose bisphosphate carboxylase (3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) has been placed under the transcriptional control of the bacteriophage lambda promoter PL, by fusion with the lambda N operon located on a multicopy plasmid. Transcription from PL was repressed at 32 degrees C by the presence in the E. coli chromosome of a cIts gene that specifies a temperature-sensitive repressor. After inactivation of the repressor at 45 degrees C unmoderated transcription of the chloroplast gene occurred from the PL promoter. Translation was probably initiated from a chloroplast Shine-Dalgarno sequence located five nucleotides from the N-terminal methionine initiation codon to yield a polypeptide the same size as that synthesised in maize. This direct translation results in a level of expression of the chloroplast gene corresponding to approximately 2% of the total E. coli cell protein as ribulose bisphosphate carboxylase large subunits. Transcriptional fusions with the lambda N operon should provide a generally applicable, simple method for the amplification and regulation of chloroplast gene expression in E. coli.
Mol Gen Genet 1982
PMID:Amplification of maize ribulose bisphosphate carboxylase large subunit synthesis in E. coli by transcriptional fusion with the lambda N operon. 621 53

A selective modification of external SH-groups of riboluse 1,5-diphosphate carboxylase (EC 4.1.1.39) from spinach by a spin label on the basis of maleimide was performed. From the EPR spectra of spin labels of three types of SH-groups were classified. It is shown that part of spin labels pre-reduced with dithiothreitol are reoxidized by the enzyme after the removal of dithiothreitol from the reaction mixture. The reoxidation is connected with the fact that one of the spin labels is bound to the SH-group at the enzyme active site and can act as its substrate, which results in alteration of the electron structure of the greater than N--O fragment in the spin label upon interaction of the spin-labeled enzyme with the substrate and Mg2+.
Mol Biol (Mosk)
PMID:[Interaction of ribulose-1,5-diphosphate carboxylase with ribulose-1,5-diphosphate and with the magnesium ion by the spin label method]. 630 90

We have examined the nuclear genes encoding the small subunit of ribulose-1,5-bisphosphate (RuBP) carboxylase from soybean. One member of this gene family, designated SRS1, has been isolated from a soybean DNA library constructed in the lambda vector Charon 4A. The complete nucleotide sequence and structure of this gene including its two introns and portions of the 5' and 3' flanking sequences were determined. The first exon encodes the entire transit peptide (55 amino acids) and the first 2 amino acids of the mature sequence. Based on analysis of the nucleotide sequence, we concluded that the precursor of the soybean small subunit consists of 178 amino acids. A gene-specific probe for SRS1 was used to show that this gene is transcribed and that steady-state levels of its transcript are strongly light regulated. S1 nuclease mapping was used to locate the potential start of transcription in the sequence and showed that the small subunit gene contains a cap site, TATA box, and -80 sequence, which match the consensus animal sequences. The mature SRS1 small subunit polypeptide of 123 amino acids contains 30 and 34 amino acid replacements relative to the previously determined amino acid sequences from pea and spinach, respectively. Southern blotting of restriction digests of soybean nuclear DNA and data on the complete structure of SRS1 suggest that a multigene family of at least 10 members encodes the RuBP carboxylase small subunit in soybean. Quantitative evolutionary comparison of the soybean small subunit sequence for SRS1 and the pea small subunit sequence suggests that these two genes diverged long before the divergence of pea and soybean.
J Mol Appl Genet 1982
PMID:The nucleotide sequence, expression, and evolution of one member of a multigene family encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in soybean. 715 86

DNA sequences of the gene tufA, encoding elongation factor Tu, were determined from five cyanobacteria and 21 plastids. Three were full-length (ca. 1230 bp) sequences from cloned DNA, and 23 were partial (ca. 740 bp) sequences from PCR fragments. These sequences were aligned with sequences available from the literature, creating a data set of 56 tufA sequences of eubacterial or plastid origin. Phylogenetic analysis was performed on inferred amino acid sequences with parsimony and neighbor joining techniques, and on first and second position nucleotide sequences with maximum likelihood, and bootstrapping was performed with each method. Trees determined by the three methods were highly congruent with respect to well supported nodes. All examined plastids, including those of green and red algae, chromophytes, and Cyanophora paradoxa, cluster strongly with the cyanobacteria in all analyses. A cyanobacterial origin of all plastids confirms phylogenetic analyses of 16S rRNA and atpB sequences, but conflicts with those of rbcL and rbcS sequences. This discrepancy may be attributable to an ancient gene transfer of the rubisco operon in an ancestor of red algae and chromophytes. Maximum likelihood analysis also provides some support for a monophyletic origin of all plastids, while neighbor joining and parsimony analyses showed cyanobacteria and red, brown, and green plastid lineages as an unresolved polytomy. These tufA analyses also provide a broad perspective on eubacterial evolution and, in conjunction with published rRNA trees, point to at least two major radiations within eubacteria and their descendants: one of many eubacterial phyla, a second of cyanobacteria, and possibly a third radiation early in plastid evolution.
Mol Phylogenet Evol 1995 Jun
PMID:Phylogenetic analysis of tufA sequences indicates a cyanobacterial origin of all plastids. 766 57

In the protist Euglena gracilis, the small subunit of the chloroplast enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase is encoded by nuclear rbcS genes and synthesized as a polyprotein precursor containing eight mature small subunit molecules. This large precursor is encoded by at least eight different nuclear genes as ascertained by transcript analysis. The structure of three rbcS genes was established and the coding sequences were found to be interrupted by many intervening sequences (IVS). Apart from the first 5' intron involved in trans-splicing, none of these IVSs obeys the GT-AG rule characteristic of introns in higher eukaryote genes. Surprisingly, these IVSs are located at identical positions within the three genes studied. Moreover, extensive sequence homologies were found between IVSs located in the same gene as well as in different genes. The sequences of these homologous IVSs differ only by inserted and/or deleted sequences. The striking conservation of the 5' and 3' regions of these IVSs is correlated to their potential secondary structures. These structures, which bring the IVS extremities together with the exon boundaries, could be involved in a novel splicing process. The second 5' IVS is shown to be excised before the addition of the spliced leader sequence to the pre-mRNA. Similarly, two 3' IVSs are excised before the polyadenylation step. These results suggest that IVS splicing is faster than eukaryotic genomic cis-splicing and involves components other than those of the classical spliceosomes.
J Mol Biol 1995 Jan 06
PMID:Structure and expression of Euglena gracilis nuclear rbcS genes encoding the small subunits of the ribulose 1,5-bisphosphate carboxylase/oxygenase: a novel splicing process for unusual intervening sequences? 782 17

The Mud technology of Groisman and Casadaban was adapted to the cyanobacterium Synechococcus sp. PCC 7942. A new high-CO2-requiring (hcr) mutant, hcr Mu28 was isolated following the integration of the Mud element 89 bp upstream of ORFI, at the 5'-flanking region of the rbc operon, which encodes RuBP carboxylase/oxygenase (Rubisco). The integration involved a 7 bp duplication that formed a direct repeat at the integration site, as previously shown in Escherichia coli. The mutant was devoid of apparent carboxysome bodies, which are considered to be important for the availability of CO2 for Rubisco. Immunolabelling studies demonstrated that Rubisco was distributed throughout hcr Mu28 cells, while in the wild type (WT) and in the carboxysome aberrant mutant hcr O221, Rubisco was markedly associated with the carboxysomes. Rubisco activase, however, was evenly distributed throughout the cytosol of the hcr and WT cells, without any preferential association with the apparent carboxysomes.
Mol Microbiol 1993 Sep
PMID:Rubisco but not Rubisco activase is clustered in the carboxysomes of the cyanobacterium Synechococcus sp. PCC 7942: Mud-induced carboxysomeless mutants. 793 32

The coding region for the Escherichia coli groEL (chaperonin-60) polypeptide was fused downstream of a pea rubisco small subunit transit peptide coding sequence under the control of a tandem 35S CaMV promoter. Transgenic tobacco plants (Nicotiana tabacum cv. Xanthi) containing this modified groEL gene were produced. The modified groEL polypeptide was correctly imported into chloroplasts and accumulated to high or low levels in different plants. The majority of the modified groEL polypeptide was processed correctly to the mature form within the chloroplasts. Approximately 20% of the imported polypeptides retained a portion of the N-terminal transit peptide (TPgroEL). Both groEL and TPgroEL polypeptides assembled into tetradecameric species in the chloroplasts. In plants accumulating high levels of these products, the majority of the plant chaperonin-60 polypeptides in the chloroplast were present in novel hybrid tetradecameric species containing both bacterial and plant chaperonin-60 polypeptides. In plants accumulating low levels of groEL, the predominant species present appeared to be authentic plant cpn60(14) and authentic bacterial groEL14. The growth and development of transgenic and control tobacco plants were indistinguishable.
Plant Mol Biol 1993 Sep
PMID:A modified Escherichia coli chaperonin (groEL) polypeptide synthesized in tobacco and targeted to the chloroplasts. 810 28


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