Arx1 Functions as an Unorthodox Nuclear Export Receptor for the 60S Preribosomal Subunit

Bradatsch, Bettina; Katahira, Jun; Kowalinski, Eva; Bange, Gert; Yao, Wei; Sekimoto, Takeyuki; Baumgärtel, Viola; Boese, G.; Baßler, Jochen; Wild, Klemens; Peters, Reiner; Yoneda, Yoshihiro; Sinning, I.; Hurt, Ed

doi:10.1016/j.molcel.2007.06.034

Cited by 107 publications

(119 citation statements)

References 54 publications

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“…However, we have no proof that the purified Nup192 has a native conformation. As previously described, Nup100 physically interacted with Arx1 (Allen et al 2002;Bradatsch et al 2007;Hung et al 2008) but not with Ecm1 in a two-hybrid and in an in vitro GST interaction assay (data not shown).…”

Section: Ecm1 Is Physically Associated With Nuclear Pore Componentssupporting

confidence: 73%

Ecm1 is a new pre-ribosomal factor involved in pre-60S particle export

Yao¹,

Demoinet²,

Saveanu³

et al. 2010

RNA

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In eukaryotes, ribosome biogenesis is a highly conserved process that starts in the nucleus and ends in the cytoplasm. In actively growing yeast cells, it is estimated that each nuclear pore complex (NPC) contributes to the export of about 25 pre-ribosomal particles per minute. Such an extremely active process requires several redundant export receptors for the pre-60S particles. Here, we report the identification of a novel pre-60S factor, Ecm1, which partially acts like Arx1 and becomes essential when the NPC function is affected. Ecm1 depletion, combined with the deletion of NPC components led to pre-60S retention in the nucleus. Functional links that we identified between Ecm1, 60S biogenesis, pre-60S export, and the NPC were correlated with physical interactions of Ecm1 with pre-60S particles and nucleoporins. These results support that Ecm1 is an additional factor involved in pre-60S export. While Ecm1 and Arx1 have redundant functions, overproduction of either one could not complement the absence of the other, whereas overproduction of Mex67 was able to partially restore the growth defect resulting from the absence of Ecm1 or Arx1. These data highlight the involvement of many factors acting together to export pre-60S particles.

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Section: Ecm1 Is Physically Associated With Nuclear Pore Componentssupporting

confidence: 73%

Ecm1 is a new pre-ribosomal factor involved in pre-60S particle export

Yao¹,

Demoinet²,

Saveanu³

et al. 2010

RNA

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“…To gain the desired in-depth structural insight into the architecture of the nascent 60S subunit, we have now determined the structure of an Arx1 particle 23 , affinity-purified via the bait protein Alb1 (ref. 22), by cryo-EM at sub-nanometre (8.7 Å) resolution ( Fig.…”

Section: Resultsmentioning

confidence: 99%

60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle

et al. 2014

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During eukaryotic ribosome biogenesis, nascent ribosomal RNA (rRNA) forms pre-ribosomal particles containing ribosomal proteins and assembly factors. Subsequently, these immature rRNAs are processed and remodelled. Little is known about the premature assembly states of rRNAs and their structural rearrangement during ribosome biogenesis. Using cryo-EM we characterize a pre-60S particle, where the 5S rRNA and its associated ribosomal proteins L18 and L5 (5S ribonucleoprotein (RNP)) are rotated by almost 180°when compared with the mature subunit. Consequently, neighbouring 25S rRNA helices that protrude from the base of the central protuberance are deformed. This altered topology is stabilized by nearby assembly factors (Rsa4 and Nog1), which were identified by fitting their three-dimensional structures into the cryo-EM density. We suggest that the 5S RNP performs a semicircular movement during 60S biogenesis to adopt its final position, fulfilling a chaperone-like function in guiding the flanking 25S rRNA helices of the central protuberance to their final topology.

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“…At least five proteins (Arx1, Bud20, Ecm1, Mex67, and Nmd3) function together to enable nuclear export of pre-60S subunits Gadal et al 2001b;Bradatsch et al 2007;Yao et al 2007Yao et al , 2010Hung et al 2008;Bassler et al 2012).…”

Section: Nuclear Export Of Pre-40s and Pre-60s Particlesmentioning

confidence: 99%

Ribosome Biogenesis in the YeastSaccharomyces cerevisiae

2013

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Ribosomes are highly conserved ribonucleoprotein nanomachines that translate information in the genome to create the proteome in all cells. In yeast these complex particles contain four RNAs (.5400 nucleotides) and 79 different proteins. During the past 25 years, studies in yeast have led the way to understanding how these molecules are assembled into ribosomes in vivo. Assembly begins with transcription of ribosomal RNA in the nucleolus, where the RNA then undergoes complex pathways of folding, coupled with nucleotide modification, removal of spacer sequences, and binding to ribosomal proteins. More than 200 assembly factors and 76 small nucleolar RNAs transiently associate with assembling ribosomes, to enable their accurate and efficient construction. Following export of preribosomes from the nucleus to the cytoplasm, they undergo final stages of maturation before entering the pool of functioning ribosomes. Elaborate mechanisms exist to monitor the formation of correct structural and functional neighborhoods within ribosomes and to destroy preribosomes that fail to assemble properly. Studies of yeast ribosome biogenesis provide useful models for ribosomopathies, diseases in humans that result from failure to properly assemble ribosomes. TABLE OF CONTENTS Abstract 643Introduction 644

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Arx1 Functions as an Unorthodox Nuclear Export Receptor for the 60S Preribosomal Subunit

Cited by 107 publications

References 54 publications

Ecm1 is a new pre-ribosomal factor involved in pre-60S particle export

Ecm1 is a new pre-ribosomal factor involved in pre-60S particle export

60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle

Ribosome Biogenesis in the YeastSaccharomyces cerevisiae

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