Related Experiment Video

Updated: Aug 11, 2026

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
08:04

DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling

Published on: October 8, 2019

p140/c-Abl that binds DNA is preferentially phosphorylated at tyrosine residues

R Dikstein1, R Agami, D Heffetz

  • 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|March 19, 1996
PubMed

Insights

Phosphorylation is crucial for p140/c-Abl protein binding to the EP DNA element. This study reveals that p140/c-Abl is a tyrosine phosphoprotein in vivo, essential for DNA-protein complex formation.

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein Biochemistry

Background:

  • The EP DNA element is present in enhancer and promoter regions of genes.
  • The p140/c-Abl protein specifically binds to the EP DNA element.

Purpose of the Study:

  • To investigate the role of phosphorylation in p140/c-Abl DNA binding activity.
  • To characterize the phosphorylation status of p140/c-Abl associated with EP DNA in vivo.
  • To identify distinct populations of c-Abl in cellular extracts.

Main Methods:

  • 32P labeling of cells
  • Protein purification
  • Western blotting using c-Abl antibodies

Main Results:

  • Phosphorylation is essential for p140/c-Abl DNA binding and DNA-protein complex formation.
  • In vivo, EP-DNA-associated p140/c-Abl is a tyrosine phosphoprotein.
  • Two distinct c-Abl populations exist in cellular extracts; p140/c-Abl is a minor, heavily phosphorylated population active in autophosphorylation.

Conclusions:

  • Phosphorylation regulates p140/c-Abl's interaction with the EP DNA element.
  • p140/c-Abl is a key tyrosine phosphoprotein involved in gene regulation via EP DNA.
  • Distinct c-Abl populations exhibit differential phosphorylation and activity.

More Related Videos

CD Spectroscopy to Study DNA-Protein Interactions06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

Related Concept Videos

Phosphorylation01:02

Phosphorylation

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...