Post translational modification occurs in ribosomes.
They in fact do. Check out a review "Postranslational Protein Modification in Archaea" by Jerry Eichler. The problem is that took a long time to discover this so it was assumed that they don't have any PTMs but this is wrong.
One way to control an enzyme is through post-translational modification such as phosphorylation or glycosylation. Other ways to control enzymes are through enzyme induction, inhibition, or by compartmentalizing the metabolic pathways.
Eukaryotes exhibit control mechanisms at all levels, including transcriptional, transcript processing, translational, and post-translational regulation. These mechanisms work together to finely regulate gene expression and protein production in response to various internal and external signals.
Post-translation or Post-translational regulation refers to the control of the levels of active protein either by means of reversible events (Post-translational modifications, such as Phosphorylation or sequestration) or by means of irreversible events (proteolysis).
The correct order of protein synthesis is transcription (DNA is copied into mRNA), translation (mRNA is decoded to build a protein), and post-translational modification (protein may undergo changes like folding or addition of functional groups).
methylation lipidation glycosylation phosphorylation
assembly of the virus particles and post-translational modification of the viral proteins.
The Golgi apparatus is primarily responsible for modifying, sorting, and packaging proteins and lipids synthesized in the endoplasmic reticulum. It processes these molecules by adding carbohydrate groups (glycosylation) and ensuring they are correctly directed to their final destinations, such as lysosomes, the cell membrane, or for secretion outside the cell. This organelle plays a critical role in the post-translational modification of proteins, which is essential for their functionality.
A peptide or protein. Sometimes in their "inactive" form and requiring a "post-translational modification" in order to get their full biological activity.
Protein synthesis consists of three main parts: transcription, translation, and post-translational modification. During transcription, the DNA sequence of a gene is copied into messenger RNA (mRNA) in the nucleus. Next, during translation, the mRNA is read by ribosomes in the cytoplasm to assemble amino acids into a polypeptide chain, forming a protein. Finally, post-translational modification involves the folding and chemical modification of the protein to achieve its functional form.
The advantages of hybridisation include: precise anatomical localisation is able to be acheived High sensitivity Disadvantages: Non-specific labelling may occur cannot provide inormation on translational and post-translational modification peace
The addition of a lactose molecule to the Lac repressor protein is an example of post-translational control in lac operon regulation. This modification prevents the Lac repressor from binding to the operator region, allowing for the transcription of the genes involved in lactose metabolism.
The organelle that resembles a stack of pancakes and is responsible for packaging and distributing molecules made in the endoplasmic reticulum (ER) is the Golgi apparatus. It modifies, sorts, and packages proteins and lipids for secretion or for use within the cell. The Golgi apparatus plays a crucial role in the post-translational modification of proteins, ensuring they are properly processed for their functions.
True. The Golgi apparatus is an important organelle responsible for modifying, sorting, and packaging proteins into vesicles for transport to their final destination within the cell or outside of the cell. It is involved in post-translational modifications, such as glycosylation, that are crucial for the functionality of many proteins.
They in fact do. Check out a review "Postranslational Protein Modification in Archaea" by Jerry Eichler. The problem is that took a long time to discover this so it was assumed that they don't have any PTMs but this is wrong.
N-glycosylation is a post-translational modification process where carbohydrate moieties are attached to the nitrogen atom of asparagine residues in proteins. This modification typically occurs in the endoplasmic reticulum (ER) and continues in the Golgi apparatus, playing a crucial role in protein folding, stability, and cellular signaling. N-glycosylation is essential for the proper function of many glycoproteins, which are involved in various biological processes.
Actually, for some uses prokaryotic cells are just fine for eukaryotic gene expression. That said bacteria are deficient in quite a lot of the post-translational modification systems that eukaryotes use, such as glycosylation. Since those post-translational modifications can actually be important to the protein's function you might choose a eukaryotic expression system to preserve them.