Answer:
Phosphorylation within the nuclear export signal interferes with the function of the signal.
Explanation:
In biochemistry, phosphorylation is the addition of a phosphate group (PO4) to a protein or other molecule. Phosphorylation is a major player in protein regulation mechanisms, preventing protein-catalyzed reaction product from accumulating in the body causing problems.
However, in some cases phosphorylation may cause nuclear accumulation of a protein in the nucleus of the cell. An example of this is the protein shown in the question above. In this case, phosphorylation in the nuclear export signal interferes with the signal function, resulting in protein accumulation in the nucleus.
Answer:
Repair mechanism for base cleavage (BER)
Explanation:
Repair by base cleavage (BER)
The altered bases are specifically recognized by glycosylases and removed, generating an AP site. The hole is filled by a DNA polymerase that takes the healthy strand as a template. This system arises not only by exposure to external agents, but also by the cell's own activity.
In case of damage in more than one nucleotide, repair by nucleotide excision (NER) is performed.
Nucleotide excision repair (NER)
The damaged area is recognized by UvrA and B, then A and B separate and UvrC enters which forms a complex with endonuclease activity with B. This enzyme cuts the T-dimer and the gap is filled by a DNA polymerase. There is also the TC-NER system (transcription-coupled nucleotide repair system). The alteration of these mechanisms gives rise to diseases such as: Xeroderma pigmentosum, Trichotiodystrophy or Cockayne Syndrome
Answer:
Habitat/Environment. Either can be right
Answer:
c. Both A and B are correct
Explanation:
Punnett squares are in the image
