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uridine/solanum tuberosum
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Orotate leads to a specific increase in uridine nucleotide levels and a stimulation of sucrose degradation and starch synthesis in discs from growing potato tubers
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Freshly cut discs from growing potato tubers were incubated for 3 h with 10 mM orotate or 10 mM uridine. Control discs incubated without precursors showed a 30-40% decrease of uridine nucleotides, but not of adenine nucleotides. Orotate- and uridine-feeding led to a 1.5- to 2-fold increase in the
Identification of lysyl residues located at the substrate-binding site in UDP-glucose pyrophosphorylase from potato tuber: affinity labeling with uridine di- and triphosphopyridoxals.
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Uridine di- and triphosphopyridoxals were used to probe the substrate-binding site in potato tuber UDP-glucose pyrophosphorylase (EC 2.7.7.9). The enzyme was rapidly inactivated in time- and dose-dependent manners when incubated with either reagent followed by reduction with sodium borohydride. The
Uridine diphosphate glucose breakdown is mediated by a unique enzyme activated by fructose 2,6-bisphosphate in Solanum tuberosum.
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In the presence of inorganic phosphate, uridine 5'-diphosphate glucose (UDPG) is specifically hydrolyzed to glucose 1-phosphate and UDP by a unique enzyme, UDPG phosphorylase. The activity of the enzyme was maximally stimulated by fructose 2,6-bisphosphate, a regulatory metabolite recently
The intracellular distribution of uridine diphosphate glucose starch synthetase in potato tubers.
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Effect of cetyltrimethylammonium bromide on the activity of particulate starch synthetase from potato tuber.
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The action of some detergents on the incorporation of glucose from uridine diphosphate glucose or adenosine diphosphate glucose into the potato tuber starch grain was studied. It was found that the cationic detergent, cetyltrimethylammonium bromide, produces a rapid binding of both sugar nucleotides
Studies on the primary and secondary structure of potato spindle tuber viroid: products of digestion with ribonuclease A and ribonuclease T1, and modification with bisulfite.
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Potato spindle tuber viroid (PSTV), a small infectios RNA, has been completely digested with RNase T1 and RNase A, and the resulting oligonucleotides have been sequenced using 5'-terminal 32p-labelling with gamma-32p ATP and T4 polynucleotide kinase, fingerprinting and controlled nuclease P1
Coconut tinangaja viroid: sequence homology with coconut cadang-cadang viroid and other potato spindle tuber viroid related RNAs.
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The nucleotide sequence of two variants of coconut tinangaja viroid (CTiV) were obtained. Both sequence variants are 254 nucleotide residues in size but differ in sequence at two positions. In comparisons with other viroids, the sequences and proposed secondary structure of CTiV show most homology
Plant cell suspension cultures sustain long-term replication of potato spindle tuber viroid.
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Cell suspension cultures were established from tomato plants (Lycopersicum esculentum cv. "Rutgers") infected with either a severe (TPS cell line) or a mild (TPM cell line) strain of potato spindle tuber viroid (PSTV) and from uninfected plants (TH cell line). Based on measurements of packed cell
The dimerization domain of potato spindle tuber viroid, a possible hallmark for infectious RNA.
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Covalently closed circular (+) RNA of the potato spindle tuber viroid (PSTVd) can efficiently dimerize noncovalently upon heating and slow cooling in the presence of monovalent cations or Mg2+. In vitro transcription of subgenomic fragments reveals that the ability to dimerize resides in the "upper
Diurnal changes in sucrose, nucleotides, starch synthesis and AGPS transcript in growing potato tubers that are suppressed by decreased expression of sucrose phosphate synthase.
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Sucrose export from leaves is high during the day and lower at night, when it depends on starch remobilisation. We have investigated the consequences of diurnal changes of photoassimilate supply for starch synthesis and other metabolic processes in growing potato tubers. Sucrose, the levels of the
Comparative affinity labeling with reactive UDP-glucose analogues: possible locations of five lysyl residues around the substrate bound to potato tuber UDP-glucose pyrophosphorylase.
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By using two reactive analogues of UDP-Glc, uridine di- and triphosphopyridoxals, we have recently probed the substrate-binding site in potato tuber UDP-Glc pyrophosphorylase [EC 2.7.7.9]. In this work, pyridoxal diphospho-alpha-D-glucose was used for the same purpose. This compound is also a
A redox switch and phosphorylation are involved in the post-translational up-regulation of the adenosine-uridine binding factor by phorbol ester and ionophore.
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Messenger RNAs coding for cytokines and lymphokines are extremely unstable due to an AU-rich cis element located in their 3'-untranslated region. Cell activation with phorbol ester 12-O-tetradecanoylphorbol-13-acetate or calcium ionophore has been shown to markedly stabilize these normally labile
Inhibition of de novo pyrimidine synthesis in growing potato tubers leads to a compensatory stimulation of the pyrimidine salvage pathway and a subsequent increase in biosynthetic performance.
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Pyrimidine nucleotides are of general importance for many aspects of cell function, but their role in the regulation of biosynthetic processes is still unclear. In this study, we investigate the influence of a decreased expression of UMP synthase (UMPS), a key enzyme in the pathway of de novo
Regulation of sucrose to starch conversion in growing potato tubers.
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Growing potato tubers have been used as a model system to investigate the regulation of starch synthesis. Results indicate that sucrose degradation and starch synthesis are controlled via regulatory signals in response to sucrose and oxygen availability. (i) Sucrose leads to a co-ordinated
An eight-nucleotide sequence in the potato virus X 3' untranslated region is required for both host protein binding and viral multiplication.
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Gel retardation and UV-cross-linking techniques were used to demonstrate that two tobacco proteins, with approximate molecular masses of 28 and 32 kDa, bind to a site within the 3' region of potato virus X (PVX) genomic RNA. The protein binding is specific, in that a 50-fold excess of unlabeled
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