The GTPase Nog1 couples polypeptide exit tunnel quality control with ribosomal stalk assembly

Nerurkar, Purnima; Gillet, Ludovic; Peña, Cohue; Schubert, Olga T.; Altvater, Martin; Chang, Yeon Soo; Aebersold, Ruedi; Panse,

doi:10.1101/462333

Cited by 5 publications

(4 citation statements)

References 61 publications

(50 reference statements)

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“…In addition, a recent study attempting to reconstitute Mex67-Mtr2 binding to affinity-purified pre-60S particles in vitro identified crosslinks to 5.8S and P-stalk rRNA (Sarkar et al 2016). However, binding to the P-stalk was only observed for Yvh1-containing pre-60S particles while our recent structural studies and work from others show that Yvh1 joins the subunit only in the cytoplasm (Kemmler et al 2009;Nerurkar et al 2018;Zhou et al 2019) and hence, cannot be responsible for promoting Mex67-Mtr2 binding to pre-60S in the nucleus.…”

Section: Introductionmentioning

confidence: 61%

“…Although the Mex67-Mtr2 duplex can bind 5S rRNA (Yao et al 2007), in vitro UV-induced crosslinking of Mex67 reconstituted with pre-60S particles affinity purified with Yvh1, identified binding sites in the P stalk and 5.8S but not 5S rRNA (Sarkar et al 2016). However, our recent structural analysis of pre-60S maturation (Zhou et al 2019) shows that Yvh1 is recruited to the pre-60S only after Nog1 is released in the cytoplasm, a conclusion reached by others as well (Nerurkar et al 2018). Thus, Yvh1 loads onto the pre-60S particle after export from the nucleus, and after the requirement for Mex67 in export.…”

Section: Quality Control and The L1 Stalkmentioning

confidence: 69%

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The L1 stalk is required for efficient export of nascent large ribosomal subunits in yeast

Musalgaonkar

Black

Johnson

2019

RNA

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The ribosomal protein Rpl1 (uL1 in universal nomenclature) is essential in yeast and constitutes part of the L1 stalk which interacts with E site ligands on the ribosome. Structural studies of nascent pre-60S complexes in yeast have shown that a domain of the Crm1-dependent nuclear export adapter Nmd3, binds in the E site and interacts with Rpl1, inducing closure of the L1 stalk. Based on this observation, we decided to reinvestigate the role of the L1 stalk in nuclear export of pre-60S subunits despite previous work showing that Rpl1-deficient ribosomes are exported from the nucleus and engage in translation. Large cargoes, such as ribosomal subunits, require multiple export factors to facilitate their transport through the nuclear pore complex. Here, we show that pre-60S subunits lacking Rpl1 or truncated for the RNA of the L1 stalk are exported inefficiently. Surprisingly, this is not due to a measurable defect in the recruitment of Nmd3 but appears to result from inefficient recruitment of the Mex67-Mtr2 heterodimer.

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Section: Introductionmentioning

confidence: 61%

Section: Quality Control and The L1 Stalkmentioning

confidence: 69%

The L1 stalk is required for efficient export of nascent large ribosomal subunits in yeast

Musalgaonkar

Black

Johnson

2019

RNA

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“…factor. The translocation of large cargo molecules through the nuclear pore complex that Yvh1 is recruited to the pre-60S only after Nog1 is released in the cytoplasm, a 8 conclusion reached by others as well (Nerurkar et al 2018). Thus, Yvh1 loads onto the 9 pre-60S particle after export from the nucleus, and after the requirement for Mex67 in 10 export.…”

Section: Resolvedmentioning

confidence: 82%

The L1 stalk is required for efficient export of nascent large ribosomal subunits in yeast

Musalgaonkar

Black

Johnson

2019

Preprint

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1The ribosomal protein Rpl1 (uL1 in universal nomenclature) is essential in yeast and 2 constitutes part of the L1 stalk which interacts with E site ligands on the ribosome. 3Structural studies of nascent pre-60S complexes in yeast have shown that a domain of 4 the Crm1-dependent nuclear export adapter Nmd3, binds in the E site and interacts with 5Rpl1, inducing closure of the L1 stalk. Based on this observation, we decided to 6 reinvestigate the role of the L1 stalk in nuclear export of pre-60S subunits despite previous 7work showing that Rpl1-deficient ribosomes are exported from the nucleus and engage 8 in translation. Large cargoes, such as ribosomal subunits, require multiple export factors 9 to facilitate their transport through the nuclear pore complex. Here, we show that pre-60S 10 subunits lacking Rpl1 or truncated for the RNA of the L1 stalk are exported inefficiently. 11 Surprisingly, this is not due to a measurable defect in recruitment of Nmd3 but appears 12 to result from inefficient recruitment of the Mex67-Mtr2 heterodimer. 13

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“…Still, the removal of Nog1 seems to be temporally tightly linked to the release of Rlp24 and can only occur when Drg1 is functional [85,166,183]. Due to the tight entanglement of these proteins, extraction of the C-terminal tail of Nog1 from the PET has been proposed to be triggered by the removal of Rlp24, while the N-terminus of Nog1 is only removed after GTP hydrolysis [189]. This hypothesis awaits testing by structural analysis.…”

Section: From the Nucleolus To The Cytoplasm: Mechanistic Insightsmentioning

confidence: 99%

Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis

Prattes

Bergler

et al. 2019

Biomolecules

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AAA-ATPases are molecular engines evolutionarily optimized for the remodeling of proteins and macromolecular assemblies. Three AAA-ATPases are currently known to be involved in the remodeling of the eukaryotic ribosome, a megadalton range ribonucleoprotein complex responsible for the translation of mRNAs into proteins. The correct assembly of the ribosome is performed by a plethora of additional and transiently acting pre-ribosome maturation factors that act in a timely and spatially orchestrated manner. Minimal disorder of the assembly cascade prohibits the formation of functional ribosomes and results in defects in proliferation and growth. Rix7, Rea1, and Drg1, which are well conserved across eukaryotes, are involved in different maturation steps of pre-60S ribosomal particles. These AAA-ATPases provide energy for the efficient removal of specific assembly factors from pre-60S particles after they have fulfilled their function in the maturation cascade. Recent structural and functional insights have provided the first glimpse into the molecular mechanism of target recognition and remodeling by Rix7, Rea1, and Drg1. Here we summarize current knowledge on the AAA-ATPases involved in eukaryotic ribosome biogenesis. We highlight the latest insights into their mechanism of mechano-chemical complex remodeling driven by advanced cryo-EM structures and the use of highly specific AAA inhibitors.

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The GTPase Nog1 couples polypeptide exit tunnel quality control with ribosomal stalk assembly

Cited by 5 publications

References 61 publications

The L1 stalk is required for efficient export of nascent large ribosomal subunits in yeast

The L1 stalk is required for efficient export of nascent large ribosomal subunits in yeast

The L1 stalk is required for efficient export of nascent large ribosomal subunits in yeast

Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis

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