The exosome, plugged

Autor: Karl-Peter Hopfner, Sophia Hartung
Rok vydání: 2007
Předmět:
Zdroj: EMBO reports. 8(5)
ISSN: 1469-221X
Popis: The correct processing, quality control and turnover of cellular RNA molecules is crucial to many aspects of cell physiology. The exosome—a large molecular assembly with exoribonuclease activity—has emerged as a crucial component in many, if not most, stages of RNA metabolism, including degradation and maturation of ribosomal RNA, RNA quality control and turnover of cytosolic messenger RNA (reviewed by Houseley et al , 2006). Exosomes are found in eukaryotes and archaea. The eukaryotic core exosome consists of six polypeptides with sequence similarity to the phosphate‐dependent 3‘→5’ exoribonuclease RNase PH and three protein K homology (KH) and/or S1‐domain‐containing RNA‐binding proteins (Fig 1A; Mitchell et al , 1997). Additional subunits include the RNase R homologue Rrp44/Dis3 (yeast exosome) and the RNase D homologue Rrp6 (nuclear isoform). The archaeal (a) exosome exhibits a simplified subunit composition and is assembled from three copies each of two RNase PH‐like proteins (aRrp41 and aRrp42), aRrp4 or aCsl4 (Evguenieva‐Hackenberg et al , 2003). Figure 1. Comparison of exosomes in archaea and eukaryotes. ( A ) Schematic comparison of subunit composition of archaeal, human and yeast exosomes (viewed from the caps of Rrp4/Rrp40/Csl4). Identified active sites are indicated by black (phosphorolytic) or white (hydrolytic) asterisks. Inactive phosphorolytic subunit pairs are shaded grey. The position of Rrp6 is inferred from native mass spectrometry (Hernandez et al , 2006). Archaeal (a) exosomes might have additional subunits and mixed aRrp4/aCsl4 trimers …
Databáze: OpenAIRE