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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
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Cell division is essential for organismal growth and development. In animal cells, the central spindle and its associated proteins form the midbody, a structure that has an essential role in cytokinesis. In plants, the central spindle, along with the microtubules, actin, and other cell components, matures into the phragmoplast, which is necessary for cytokinesis. Unlike the stationary midbody, the phragmoplast expands centrifugally, eventually leading to the formation of the new cell wall.
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Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
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Related Experiment Video

Updated: May 5, 2026

Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates
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Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates

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Polynucleotide phosphorylase from plant cells.

E Schumacher-Wittkopf1, G Richter, S Schulze

  • 1Institut für Botanik der universität Hannover, Herrenhäuser Straße 2, D-3000, Hannover, Federal Republic of Germany.

Plant Cell Reports
|November 21, 2013
PubMed
Summary

Polynucleotide phosphorylase was isolated from parsley and tomato cells. This enzyme has five subunits, with one subunit identified as a glycoprotein.

Area of Science:

  • Plant Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Polynucleotide phosphorylase (PNPase) plays a crucial role in RNA metabolism in various organisms.
  • Understanding PNPase in plants is essential for comprehending gene expression regulation and RNA processing.
  • Previous research on plant PNPase structure and function is limited, necessitating further investigation.

Purpose of the Study:

  • To isolate and characterize polynucleotide phosphorylase from plant sources.
  • To determine the subunit composition and properties of plant PNPase.
  • To provide a foundation for future studies on plant RNA metabolism.

Main Methods:

  • Enzyme isolation from suspension-cultured parsley cells and tomato seedlings.
  • Purification using ultracentrifugation, glycerol density gradient centrifugation, and preparative gel electrophoresis.

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  • Characterization by isoelectric focusing and SDS-PAGE to determine subunit molecular weights.

    • Main Results:

    • Successfully isolated polynucleotide phosphorylase from both parsley and tomato.
    • Isoelectric focusing revealed a major component (pI ≈ 7.5) and a minor component (pI ≈ 5).
    • The enzyme comprises five subunits with apparent molecular masses of 160,000, 140,000, 70,000, 34,000, and 12,000 Da; the 70,000-Da subunit is a glycoprotein.

    Conclusions:

    • The study describes a robust method for plant polynucleotide phosphorylase isolation.
    • The identified subunit composition provides insights into the enzyme's structure.
    • The characterization of a glycoprotein subunit opens avenues for studying post-translational modifications in plant PNPase.