Adp-ribosylation
Adp-ribosylation - Related Videos
01:42
The ADP/ATP Carrier Protein
0 Views •
2023
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
01:08
Hydrolysis of ATP
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2019
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids. If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
10:44
Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
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Cited by 12 •
2018
The goal of this protocol is to describe how to use laser microirradiation to induce different types of DNA damage, including relatively simple strand breaks and complex damage, to study DNA damage signaling and repair factor assembly at damage sites in vivo.
01:28
Energy-releasing Steps of Glycolysis
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2019
Glycolysis is divided into two phases based on whether energy is utilized or released. While the first phase consumes ATP, the second phase produces energy in the form of ATP and NADH. The energy is released over a sequence of reactions that turns G3P into pyruvate. The energy-releasing phase—steps 6-10 of glycolysis—occurs twice, once for each of the two 3-carbon sugars produced during steps 1-5 of the first phase. The first energy-releasing step—the 6th step of glycolysis —consists of two...
10:25
Isolation of Intact Mitochondria from Skeletal Muscle by Differential Centrifugation for High-resolution Respirometry Measurements
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Cited by 26 •
2017
Here, a quadriceps muscle specimen is taken from an anaesthetized pig and mitochondria are isolated by differential centrifugation. Then, the respiratory rates of mitochondrial respiratory chain complexes I, II and IV are determined using high-resolution respirometry.
FAQs
NAD+ supplies the ADP-ribose group that ADP-ribosyltransferase enzymes transfer to a protein or nucleic acid. The enzyme therefore links cellular modification to the availability and use of this donor molecule. Depending on the reaction, transfer produces either a single attached unit or a growing poly(ADP-ribose) chain, creating different regulatory possibilities.
Hydrolases remove ADP-ribose from modified targets, counterbalancing the activity of ADP-ribosyltransferases. This opposing enzyme activity makes the modification reversible rather than permanent. In biochemical regulation, reversibility allows cells to adjust protein or nucleic-acid behavior as conditions change, helping control signaling, stress responses, and other processes without continuously replacing the modified molecules.
A single ADP-ribose unit and a poly(ADP-ribose) chain represent distinct modification states. The single unit changes a target directly, whereas chain formation can create a larger modified structure associated with broader changes in molecular interactions. This distinction is important when examining how ADP-ribosylation influences chromatin organization, DNA damage responses, or signaling.
The modification can affect both proteins and nucleic acids, so its consequences extend beyond regulation of protein activity alone. Attachment to these different target classes may alter their interactions or functional behavior. This broad substrate scope helps explain why ADP-ribosylation participates in coordinated regulation of transcription, protein trafficking, chromatin organization, and cellular signaling.
Researchers can examine ADP-ribosylation in relation to DNA damage responses, chromatin organization, transcription, protein trafficking, and cell signaling. These processes reveal how the modification changes molecular activity and interactions under cellular stress. Studying several contexts together helps connect enzyme-controlled modification events with genome stability and broader regulation of cell behavior.
Investigating the enzymes that add and remove ADP-ribose can clarify disease mechanisms linked to disrupted cellular regulation or genome stability. The same enzyme systems also provide potential therapeutic targets because their activities control a reversible modification. Consequently, biochemical studies can connect molecular changes in ADP-ribosylation with disease research and the development of enzyme-targeted therapies.