In this video, we're going to begin our lesson on eukaryotic post-translational regulation. And so eukaryotes can regulate expression at the post-translational level by controlling the activity of the expressed protein. Recall from our previous lesson videos that post-translational modifications can be abbreviated as PTMs. And really they are defined as covalent modifications to proteins after translation takes place, and that is what the post, root here is referring to. Post is referring to after. Now these post-translational modifications or PTMs, they can either activate or inactivate a protein depending on the specific protein in the specific scenario. Or they can actually tag the protein or mark the protein for degradation by proteases. And so proteases are specific enzymes that are going to degrade proteins by breaking polypeptide bonds, the bonds that link amino acids together. By degrading proteins, by breaking polypeptide bonds, they're capable of making single amino acids. If we take a look at our image down below, we can get a better understanding of these post-translational modifications. Protein activity can be controlled by post-translational modifications or the degradation by proteases. Taking a look at our little mini map over here, what you'll notice is post-translational protein modifications occur in the cytoplasm of the cell. Up above, what we're showing you is the mRNA here that's going to be translated into a protein. But in many cases, proteins that are initially translated can be inactive proteins. The post-translational modification here includes, this modification tag, basically covalently modifying the protein to create an active protein. This is a form of turning on gene expression to ensure that there is an active protein product. Again, this is through post-translational modification, a modification that occurs after translation has occurred. Now, again, post-translational modifications can inactivate a protein as well. So it's also a form of turning off a gene. Down below what we're showing you is, again, an mRNA being translated into a protein. And this time, there is again a modificational tag being added to the protein. But this time, this tag is actually marking the protein for degradation by this protease enzyme. And this protease enzyme in blue is going to perform protein degradation to break up that protein into individual amino acids. Of course, if we are degrading the protein, then that is a form of turning off the gene. It's a form of regulation. You can see here that through post-translational modifications, proteins can be turned on and or proteins can be turned off depending on the specific scenario. This here concludes our brief introduction to eukaryotic post-transitional regulation, and we'll be able to get some practice applying these concepts as we move forward in our course. So I'll see you all in our next video.
Eukaryotic Post-Translational Regulation - Online Tutor, Practice Problems & Exam Prep
Eukaryotic cells regulate protein activity through post-translational modifications (PTMs), which can activate or inactivate proteins after translation. Ubiquitination, a specific PTM, involves the addition of ubiquitin by ubiquitin ligase to target proteins for degradation by proteases. This process is crucial for removing misfolded or nonfunctional proteins, thereby regulating gene expression and maintaining cellular function. Understanding these mechanisms is essential for grasping cellular regulation and protein dynamics in eukaryotes.
Eukaryotic Post-Translational Regulation
Video transcript
Protein degradation is one strategy to control gene expression and is considered ______.
Post-translational modifications of proteins can affect which of the following?
Protein Ubiquitination
Video transcript
In this video, we're going to talk about protein ubiquitination. Eukaryotes need a way to remove or degrade proteins in a cell that are no longer needed. Recall from our previous lesson videos that cells can utilize post-translational modifications, or PTMs, to tag specific proteins in a cell to be degraded by cellular proteases, the enzymes that degrade proteins. In terms of ubiquitination, ubiquitin is actually a small peptide, a small fragment of protein, that is going to be used by eukaryotic cells to mark other proteins for degradation. We'll be able to see this down below in our image. Now, ubiquitin ligase is an enzyme, a cellular enzyme, that is going to add the ubiquitin peptide to target the protein for degradation. Let's take a look at our image down below to get a better understanding of this. In this example, we're looking at how ubiquitin ligase can add a ubiquitin peptide to misfolded or non-functioning proteins in order to get rid of them and remove them. Once again, this is a type of post-translational modification that occurs in the cytoplasm.
Protein ubiquitination is, basically, what you can see in this image where the mRNA strand is going to be translated into a protein, perhaps an inactive or misfolded non-functioning protein. What can happen is this enzyme, ubiquitin ligase, can take this ubiquitin molecule, this ubiquitin tag, and transfer it over to the tagged protein. Now we have a tagged protein, and this tagged protein has been tagged for degradation by the protease enzyme over here. The protease enzyme can bind to the tagged protein, and that is ultimately going to lead to protein degradation. That will remove the protein that is no longer needed, is non-functioning, or is misfolded. This is a way of regulating gene expression as well, by getting rid of proteins that are no longer needed. This here concludes our brief introduction to protein ubiquitination, and we'll be able to get some practice applying these concepts as we move forward in our course. I'll see you all in our next video.
A hormone signal reaches a cell and causes the cell to produce a large quantity of Protein X. After some time, the hormone signal disappears and the cell no longer needs a large quantity of Protein X. How will the cell remove the excess protein?