The exosome complex is a multi-protein intracellular complex capable of degrading various types of RNA molecules. Several proteins in theExosome are the target of autoantibodies in patients with specific autoimmune diseases. mutations in exosom component 3 cause pontocerebellar hypoplasia and spinal motor neuron disease.
About Exosome complex in brief
The exosome complex is a multi-protein intracellular complex capable of degrading various types of RNA molecules. Exosome complexes are found in both eukaryotic cells and archaea, while in bacteria a simpler complex called the degradosome carries out similar functions. The core of the complex has a ring structure consisting of six proteins that all belong to the same class of RNases, the RNase PH-like proteins. Several proteins in theExosome are the target of autoantibodies in patients with specific autoimmune diseases and some antimetabolic chemotherapies for cancer function by blocking the activity of the exosomes. mutations in exosom component 3 cause pontocerebellar hypoplasia and spinal motor neuron disease. In yeast, Rrp44 has a crucial role in the activity. of the complexes and resides in a separate domain of the protein 44, which is a homologue of the human homologue Rr44. In archaea there are two different PH- like proteins, each present three times in an alternating order. Eukaryotes, three different “S1” proteins are bound to the ring, whereas in archaea either one or two different”S1\’ proteins can be part of the Exosomal complex. Besides these nine proteins, two other proteins often associate with the complex, these are the endoribonucleases 3 and 3′ endides’ These proteins’ activity is associated with all exosomal complexes.
In bacteria, the protein RN enzyme PH forms a hexameric ring consisting of 6 identical RNasePH proteins. Because of this high similarity in both protein domains and structure, these complexes are thought to be evolutionarily related and have a common ancestor. In the case of PNPase, two RN enzyme domains, and both an S1 and KH RNA binding domain are part of a single protein, which forms a trimeric complex that adopts a structure almost identical to that of theexosome. The exosOME was first discovered as an RNase in 1997 in the budding yeast Saccharomyces cerevisiae, an often-used model organism. Not long after, in 1999, it was realized it was in fact the yeast equivalent of an already described complex in human cells called the PMScl complex, which had been identified as an autoantigen in certain autoimmune diseases years earlier. In 2001, the increasing amount of genome data that had become available allowed the prediction of exosite proteins in archaeA, although it would take another 2 years before the first exOSome complex from an archaeal organism was purified.
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This page is based on the article Exosome complex published in Wikipedia (as of Nov. 04, 2020) and was automatically summarized using artificial intelligence.