The antibiotics resistance gene allows selection in bacteria
Answer:
1) Ubiquitin is a relatively small protein that is widely expressed in eukaryotic cells.
2) It is covalently attached to target proteins in an ATP-dependent reaction.
4) Target selection is determined by ubiquitin-protein ligases.
Explanation:
Ubiquitin is a eukaryotic protein. It is very small in size and is highly conserved among the various species of eukaryotes. The function of ubiquitin is to mark an intracellular protein for degradation by proteasomes. Attachment of first ubiquitin to the target protein facilitates the joining of more ubiquitin molecules. The tagged protein enters proteolytic degradation. The ubiquitin molecules are covalently attached to a Lys residue in the target protein.
Ubiquitin specifically becomes covalently attached to the lysine residues of the target protein. This reaction is mediated by the ubiquitinating enzyme in an ATP dependent manner. Specific recognizing proteins recognize the target protein and facilitate the ligation of ubiquitin to target it for destruction by proteasomes.
Answer:
The circulatory system also removes carbon dioxide and waste from cells
Answer:
it will become turgid.
Explanation:
since the concentration of salt is less in the solution than the rbc ,due to osmosis more water enters the rbc hence making it turgid.
Answer:
Each objective lens has a different magnification. Multiply the magnification of the eyepiece by the magnification of the objective lens to produce total magnification. For example, a 10X ocular lens and a 40X objective lens will produce a total magnification of 400X (10 x 40 = 400).
