TLS Online TPP Program

#Id: 10255


The synthesis of Group 3 D‐7 family* LEA proteins, storage proteins, and lipids is promoted by ABA

#Unit 6. System Physiology – Plant #Abscisic Acid - A Seed Maturation and Antistress Signal #Part B Pointers
More Pointers
TLS Online TPP Program

#Id: 5918

#Unit 3. Fundamental Processes

The holoenzyme assembles on replication fork DNA in three stages:
1. First the clamp loader uses hydrolysis of ATP to bind b subunits to a template primer complex.
2. Binding to DNA changes the conformation of the site on b that binds to the clamp loader, and as a result it now has a high affinity for the core polymerase
3. A t dimer binds to the core polymerase, and provides a dimerization function that binds a second core polymerase

TLS Online TPP Program

#Id: 5919

#Unit 3. Fundamental Processes

This is equivalent to nick translation, except that the new DNA replaces a stretch of RNA rather than a segment of DNA.




TLS Online TPP Program

#Id: 5920

#Unit 3. Fundamental Processes

Trombone” model for coordinating replication by two DNA polymerases at the E. coli replication fork


TLS Online TPP Program

#Id: 5921

#Unit 3. Fundamental Processes

Each Okazaki fragment starts with a primer and stops before the next fragment

TLS Online TPP Program

#Id: 5922

#Unit 3. Fundamental Processes

The 5’–3’ exonuclease activity removes the RNA primer while simultaneously replacing it with a DNA sequence extended from the 3’–OH end of the next Okazaki fragment. 

TLS Online TPP Program

#Id: 5923

#Unit 3. Fundamental Processes

To replace the RNA primers with DNA, an enzyme called RNaseH recognizes and removes most of each RNA primer. This enzyme specifically degrades RNA that is base-paired with DNA. RNase H removes all of the RNA primer except the ribonucleotide directly linked to the DNA end.
This is because RNaseH can only cleave bonds between two ribonucleotides. The final ribonucleotide is removed by a 5’ exonuclease that degrades RNA or DNA from their 5’ ends.