Why are the NLS of proteins are not cleaved (removed) once the protein fully imports into the nucleus? Why can proteins that are targeted to other cellular organelles remove their signal sequence? Please explain!
The nuclear envelope degrades during the mitosis process and all the nuclear proteins are released into the cytoplasm. At the end of mitosis when the nuclear envelope is formed again, these proteins are needed to be transported again into the nucleus. They again entered into the nucleus and their entry is processed by the NLS. Some of these NLS signals are part of nuclear protein which are important for nuclear function.
The proteins that are targeted to other organelles only use their peptide sequence to gain entry into the organelles. After gaining entry into the organelles, these signals are removed by signal peptidase as these signals have no role in the function of Protein.
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