Poring over exosome structure

Tsanova, Borislava; Hoof, Ambro van

doi:10.1038/embor.2010.184

Cited by 3 publications

(1 citation statement)

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“…Three heterodimers of RNase PH-like domain proteins (RRP41–RRP45, MTR3–RRP42, and RRP46–RRP43) form a ring, and three proteins with S1 and/or KH RNA-binding domains (RRP4, RRP40, and CSL4) form a cap-like structure on top of the ring ( Figure 2 ; Liu et al, 2006 ). Exo9 is structurally and evolutionarily related to bacterial polynucleotide phosphorylases (PNPases) and archaeal exosomes ( Tsanova and van Hoof, 2010 ; Januszyk and Lima, 2014 ). Archaeal exosomes, consisting of three RRP41–RRP42 heterodimers, harbor three catalytic sites located at the interfaces of each dimer inside the channel ( Figure 2A ; Böttner et al, 2005 ; Lorentzen et al, 2005 ; Lorentzen and Conti, 2012 ).…”

Section: The Exosome Core Complexmentioning

confidence: 99%

Catalytic activities, molecular connections, and biological functions of plant RNA exosome complexes

Lange

Gagliardi

2021

The Plant Cell

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RNA exosome complexes provide the main 3’-5’ exoribonuclease activities in eukaryotic cells and contribute to the maturation and degradation of virtually all types of RNA. RNA exosomes consist of a conserved core complex that associates with exoribonucleases and with multimeric cofactors that recruit the enzyme to its RNA targets. Despite an overall high level of structural and functional conservation, the enzymatic activities and compositions of exosome complexes and their cofactor modules differ among eukaryotes. This review highlights unique features of plant exosome complexes, such as the phosphorolytic activity of the core complex, and discusses the exosome cofactors that operate in plants and are dedicated to the maturation of ribosomal RNA, the elimination of spurious, misprocessed and superfluous transcripts, or the removal of mRNAs cleaved by the RNA-induced silencing complex and other mRNAs prone to undergo silencing.

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