Purification and Characterization of Phosphoribosylpyrophosphate Synthetase from Rubber Tree Latex

Gallois, Richard; Prévôt, Jean-Claude; Clément, Anne; Jacob, Jean-Louis

doi:10.1104/pp.115.2.847

Cited by 13 publications

(11 citation statements)

References 22 publications

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“…For example the rat liver enzyme exists in an aggregate form composed of 34-kDa (PRSI and PRSII), 39-kDa (PAP39), and 41-kDa (PAP41) subunits in a ratio of 20:5:8:1 (55). In rubber tree latex the enzyme seems to be a tetramer (56), although the crystal structure of the Bacillus subtilis PRS has shown it to be hexameric (57) and in Salmonella typhimurium the smallest active form of PRS may be pentameric (58).…”

Section: Discussionmentioning

confidence: 99%

Genetic Analysis and Enzyme Activity Suggest the Existence of More Than One Minimal Functional Unit Capable of Synthesizing Phosphoribosyl Pyrophosphate in Saccharomyces cerevisiae

Hernando¹,

Carter²,

Parr³

et al. 1999

Journal of Biological Chemistry

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The PRS gene family in Saccharomyces cerevisiae consists of five genes each capable of encoding a 5-phosphoribosyl-1(␣)-pyrophosphate synthetase polypeptide. To gain insight into the functional organization of this gene family we have constructed a collection of strains containing all possible combinations of disruptions in the five PRS genes. Phenotypically these deletant strains can be classified into three groups: (i) a lethal phenotype that corresponds to strains containing a double disruption in PRS2 and PRS4 in combination with a disruption in either PRS1 or PRS3; simultaneous deletion of PRS1 and PRS5 or PRS3 and PRS5 are also lethal combinations; (ii) a second phenotype that is encountered in strains containing disruptions in PRS1 and PRS3 together or in combination with any of the other PRS genes manifests itself as a reduction in growth rate, enzyme activity, and nucleotide content; (iii) a third phenotype that corresponds to strains that, although affected in their phosphoribosyl pyrophosphate-synthesizing ability, are unimpaired for growth and have nucleotide profiles virtually the same as the wild type. Deletions of PRS2, PRS4, and PRS5 or combinations thereof cause this phenotype. These results suggest that the polypeptides encoded by the members of the PRS gene family may be organized into two functional entities. Evidence that these polypeptides interact with each other in vivo was obtained using the yeast twohybrid system. Specifically PRS1 and PRS3 polypeptides interact strongly with each other, and there are significant interactions between the PRS5 polypeptide and either the PRS2 or PRS4 polypeptides. These data suggest that yeast phosphoribosyl pyrophosphate synthetase exists in vivo as multimeric complex(es).The enzyme 5-phosphoribosyl-1(␣)-pyrophosphate synthetase (ATP:D-ribose-5-phosphate pyrophosphotransferase; EC 2.7.6.1) (PRS) 1 catalyzes the reaction at a key junction in intermediary metabolism. PRS transfers the pyrophosphate moiety released from ATP to ribose-5-phosphate, thus giving rise to phosphoribosyl-pyrophosphate (PRPP) (1), and the enzyme therefore directs ribose-5-phosphate from energy generated by the pentose phosphate pathway to the important biosynthetic intermediate PRPP. PRPP is a precursor for the production of purine, pyrimidine, and pyridine nucleotides and the amino acids histidine and tryptophan (2). PRPP is required for both the de novo and the salvage pathways of nucleotide metabolism (3). It has been shown that in Mycobacterium spp. PRPP is also required for the biosynthesis of polyprenylphosphate pentoses that contribute to the arabinosyl residues of the cell wall (4).PRS genes have been cloned and sequenced from a variety of organisms; bacteria (5-9), mycoplasma (10), and protozoa (11) each contain apparently one PRS gene. In nematodes (12, 13) and the yeast Schizosaccharomyces pombe (14, 15) two PRS genes have been found so far, whereas in Spinacia oleracea four PRS cDNAs have been identified (16). PRS genes have also been cloned in rat (17-20) and human (21...

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Section: Discussionmentioning

confidence: 99%

Genetic Analysis and Enzyme Activity Suggest the Existence of More Than One Minimal Functional Unit Capable of Synthesizing Phosphoribosyl Pyrophosphate in Saccharomyces cerevisiae

Hernando¹,

Carter²,

Parr³

et al. 1999

Journal of Biological Chemistry

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“…ATP functioned as a diphosphoryl donor, whereas neither GTP, CTP, nor UTP functioned as a diphosphoryl donor. Apparent K m values for ATP and ribose 5-phosphate were determined to be 0.2 M and 40 M, respectively (131). As before, the data should be reevaluated with the current knowledge of the multiple forms of PRPP synthases.…”

Section: Class II Prpp Synthasesmentioning

confidence: 99%

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance

Hove‐Jensen

Andersen

Kilstrup

et al. 2017

Microbiol Mol Biol Rev

157

187

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SUMMARY Phosphoribosyl diphosphate (PRPP) is an important intermediate in cellular metabolism. PRPP is synthesized by PRPP synthase, as follows: ribose 5-phosphate + ATP → PRPP + AMP. PRPP is ubiquitously found in living organisms and is used in substitution reactions with the formation of glycosidic bonds. PRPP is utilized in the biosynthesis of purine and pyrimidine nucleotides, the amino acids histidine and tryptophan, the cofactors NAD and tetrahydromethanopterin, arabinosyl monophosphodecaprenol, and certain aminoglycoside antibiotics. The participation of PRPP in each of these metabolic pathways is reviewed. Central to the metabolism of PRPP is PRPP synthase, which has been studied from all kingdoms of life by classical mechanistic procedures. The results of these analyses are unified with recent progress in molecular enzymology and the elucidation of the three-dimensional structures of PRPP synthases from eubacteria, archaea, and humans. The structures and mechanisms of catalysis of the five diphosphoryltransferases are compared, as are those of selected enzymes of diphosphoryl transfer, phosphoryl transfer, and nucleotidyl transfer reactions. PRPP is used as a substrate by a large number phosphoribosyltransferases. The protein structures and reaction mechanisms of these phosphoribosyltransferases vary and demonstrate the versatility of PRPP as an intermediate in cellular physiology. PRPP synthases appear to have originated from a phosphoribosyltransferase during evolution, as demonstrated by phylogenetic analysis. PRPP, furthermore, is an effector molecule of purine and pyrimidine nucleotide biosynthesis, either by binding to PurR or PyrR regulatory proteins or as an allosteric activator of carbamoylphosphate synthetase. Genetic analyses have disclosed a number of mutants altered in the PRPP synthase-specifying genes in humans as well as bacterial species.

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“…In a previous study, PRS preparations had been purified from rubber tree latex. Biochemical analysis revealed that Mg 2+ and P affected the activity of this latex PRS; and it used only ATP as the diphosphate group donor [ 18 ]. Based on the biochemical characteristics of this latex PRS and classification of PRS family proteins, it is safe to deduce that this latex PRS belongs to Class I PRS.…”

Section: Discussionmentioning

confidence: 99%

“…Energy availability, mainly constituted with the total content of adenine nucleotide, is a major factor affecting NR regeneration between two tappings [ 14 ]; while PRPP is a precursor to synthesize adenine nucleotide [ 1 ]. In earlier research, PRS preparations have been purified from rubber tree latex, which depend on Mg 2+ and P for activity, and used only ATP as the diphosphate group donor [ 18 ]. However, so far, no PRS genes have been cloned, let alone studied for their biological functions in rubber tree.…”

Section: Introductionmentioning

confidence: 99%

Identification of a Ribose-Phosphate Pyrophosphokinase that Can Interact In Vivo with the Anaphase Promoting Complex/Cyclosome

Zhang

et al. 2017

IJMS

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5-Phospho-d-ribosyl-1-diphosphate (PRPP) synthase (PRS) catalyzes the biosynthesis of PRPP, which is an important compound of metabolism in most organisms. However, no PRS genes have been cloned, let alone studied for their biological function in rubber tree. In this study, we identify a novel protein (PRS4) that interacts in vivo with rubber tree anaphase promoting complex/cyclosome (APC/C) subunit 10 (HbAPC10) by yeast two-hybrid assays. PRS4 has been cloned from rubber tree and named as HbPRS4. Blastp search in the genome of Arabidopsis thaliana showed that HbPRS4 shared the highest similarity with AtPRS4, with 80.71% identity. qRT-PCR was used to determine the expression of HbPRS4 in different tissues and under various treatments. HbPRS4 was preferentially expressed in the bark. Moreover, the expression level of HbPRS4 was significantly induced by the proteasome inhibitor MG132 treatment, suggesting it might be regulated by the ubiquitin/26S proteasome pathway. The amount of HbPRS4 transcript was obviously decreased after mechanical wounding and abscisic acid (ABA) treatments, while a slight increase was observed at 24 h after ABA treatment. HbPRS4 transcript in the latex was significantly upregulated by ethephon (ET) and methyl jasmonate (MeJA) treatments. These results suggested that HbPRS4 may be a specific substrate of HbAPC10 indirectly regulating natural rubber biosynthesis in rubber tree.

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Purification and Characterization of Phosphoribosylpyrophosphate Synthetase from Rubber Tree Latex

Cited by 13 publications

References 22 publications

Genetic Analysis and Enzyme Activity Suggest the Existence of More Than One Minimal Functional Unit Capable of Synthesizing Phosphoribosyl Pyrophosphate in Saccharomyces cerevisiae

Genetic Analysis and Enzyme Activity Suggest the Existence of More Than One Minimal Functional Unit Capable of Synthesizing Phosphoribosyl Pyrophosphate in Saccharomyces cerevisiae

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance

Identification of a Ribose-Phosphate Pyrophosphokinase that Can Interact In Vivo with the Anaphase Promoting Complex/Cyclosome

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