Functions of Nup133

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The nuclear pore complex protein Nup 133 has the ability to function in multiple ways within the structures of living things, more specifically, humans, plants and yeast. Nup 133 is a nucleoporin of the nuclear pore complex (NPC) that played a role in nuclear pore complex biogenesis and the formation of the nuclear pore complex scaffold (Berke, 2004). Nup 133 facilitated the joining of the kinetochore protein and centromere protein F (CENPF) at the nuclear envelope during prophase, which created a centrosome-anchoring network (Rosenthal, 2011). Based on an experiment conducted by Lucy Pemberton, Michael Rout and Gunter Blobel, cells that were capable of carrying a copy of the Nup 133 protein, that had been physically disturbed, became sensitive to temperatures associated with growth and experienced clustering within the nuclear pore complexes, which is considered an abnormal condition (Pemberton, 1995). By disturbing the nuclear pore complex protein Nup 133, a decrease in growth defects appeared within the cells as the temperatures within its surroundings increased (Pemberton, 1995). When referring to the concept of nuclear pore clustering, Nup 133-, a product of the nuclear pore complex protein Nup133, produced large amounts of clustering on the nuclear envelope at limited sites (Doye, 1994).
According to an experiment conducted by Valerie Doye, Roger Wepf and Eduard Hurt, the protein nup 133- assembled poly (A) + RNA within the nucleus without interfering with the import of a karyophilic reporter protein (Doye, 1994). A mutated Nup 133p, a product of the NPC protein Nup133, gathered poly (A) + RNA or modified the distribution of nuclear pores, or contributed to both situations (Doye, 1994). Nup 133- cells grew at 18°C and displayed a normal export of poly (A) + RNA into the cytoplasm (Doye, 1994). However, the growth rate of Nup 133 stopped once temperatures reach 37°C (Doye, 1994). At 37°C, nup 133- cells experienced one or two cell divisions before the cell officially stopped growing all together (Doye, 1994). Wild-type Nup133 helped aid in protecting the temperature sensitivity of nup 133- cells (Doye, 1994).
According to an experiment conducted by Sanjay Vasu et al., when both Nup 160 and Nup 133 worked together as a system, they were able to contribute to the export of mRNA into the cytoplasm and interact with nuclear complex proteins Nup 98 and Nup 153 (Vasu, 2001). However, specific fragments of Nup 160 and Nup 133 played a role in preventing the process of mRNA export in the cells of mammals (Vasu, 2001).

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