Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0

Lo, Kai-Yin; Li, Zhihua; Wang, Feng; Marcotte, Edward M.; Johnson, Arlen

doi:10.1083/jcb.200904110

Cited by 108 publications

(159 citation statements)

References 52 publications

(82 reference statements)

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“…It was postulated that the uL11 is responsible for the Yvh1 binding, a trigger factor involved in Mrt4 release from pre-60S. 28 However, our microscopic observations do not support this hypothesis. The predominant phenotype associated with Yvh1 malfunction or other conditions affecting Mrt4-P-stalk exchange is re-localization of the Mrt4 protein from the nucleus/nucleolus into the cytoplasm.…”

Section: Ribosomal Biogenesiscontrasting

confidence: 56%

“…The predominant phenotype associated with Yvh1 malfunction or other conditions affecting Mrt4-P-stalk exchange is re-localization of the Mrt4 protein from the nucleus/nucleolus into the cytoplasm. 28,38,39 We saw no signs of such abnormal Mrt4 behavior, which was found in the nuclear compartment in the wild type and in both mutants analyzed, namely the DuL11AB and DEfl1 strains (Fig. 4B).…”

Section: Ribosomal Biogenesismentioning

confidence: 95%

“…Two consecutive steps of ribosome biogenesis, namely Tif6 release by the Efl1 GTPase and the "translation-like cycle" catalyzed by the eIF5B, might be GAC dependent. 28,29 Based on sequence homology, high-resolution structures, and previous biochemical data, it is tempting to assume that the mode of functioning of Efl1 and eIF5B is similar to other trGTPases (e.g. eEF2 or eEF1A), and consequently uL11 dependent.…”

Section: Introductionmentioning

confidence: 99%

“…26,27 It is postulated that uL11 and Mrt4 are important for proper spatial organization of early GAC and subsequent Yvh1 driven P-stalk loading, which gives rise to mature GAC formation. 28 Correctly assembled GAC becomes a functional checkpoint for verification of 60S translational capacity. Two consecutive steps of ribosome biogenesis, namely Tif6 release by the Efl1 GTPase and the "translation-like cycle" catalyzed by the eIF5B, might be GAC dependent.…”

Section: Introductionmentioning

confidence: 99%

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Functional analysis of the uL11 protein impact on translational machinery

Wawiórka¹,

Molestak²,

Szajwaj³

et al. 2016

Cell Cycle

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The ribosomal GTPase associated center constitutes the ribosomal area, which is the landing platform for translational GTPases and stimulates their hydrolytic activity. The ribosomal stalk represents a landmark structure in this center, and in eukaryotes is composed of uL11, uL10 and P1/P2 proteins. The modus operandi of the uL11 protein has not been exhaustively studied in vivo neither in prokaryotic nor in eukaryotic cells. Using a yeast model, we have brought functional insight into the translational apparatus deprived of uL11, filling the gap between structural and biochemical studies. We show that the uL11 is an important element in various aspects of 'ribosomal life'. uL11 is involved in 'birth' (biogenesis and initiation), by taking part in Tif6 release and contributing to ribosomal subunit-joining at the initiation step of translation. uL11 is particularly engaged in the 'active life' of the ribosome, in elongation, being responsible for the interplay with eEF1A and fidelity of translation and contributing to a lesser extent to eEF2-dependent translocation. Our results define the uL11 protein as a critical GAC element universally involved in trGTPase 'productive state' stabilization, being primarily a part of the ribosomal element allosterically contributing to the fidelity of the decoding event.

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Section: Ribosomal Biogenesiscontrasting

confidence: 56%

Section: Ribosomal Biogenesismentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Functional analysis of the uL11 protein impact on translational machinery

Wawiórka¹,

Molestak²,

Szajwaj³

et al. 2016

Cell Cycle

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“…10 YVH1 was also recently identified as a 60S transacting factor in a mass spectrometry (MS)-based analysis of pre-60S particles. 11 An interplay between YVH1 and Mrt4 was found to be required for the late maturation step of the 60S subunit, 12,13 thus highlighting the role of YVH1 in the ribosomal biogenesis pathway.…”

Section: Introductionmentioning

confidence: 99%

The dual-specificity phosphatase hYVH1 (DUSP12) is a novel modulator of cellular DNA content

Kozarova¹,

Hudson²,

Vacratsis³

2011

Cell Cycle

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Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome

et al. 2020

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The uL10 protein is the main constituent of the ribosomal P‐stalk, anchoring the whole stalk to the ribosome through interactions with rRNA. The P‐stalk is the core of the GTPase‐associated center (GAC), a critical element for ribosome biogenesis and ribosome translational activity. All P‐stalk proteins (uL10, P1, and P2) undergo phosphorylation within their C termini. Here, we show that uL10 has multiple phosphorylation sites, mapped also within the N‐terminal rRNA‐binding domain. Our results reveal that the introduction of a negative charge within the N terminus of uL10 impairs its association with the ribosome. These findings demonstrate that uL10 N‐terminal phosphorylation has regulatory potential governing the uL10 interaction with the ribosome and may control the activity of GAC.

show abstract

Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0

Abstract: The step by step assembly process from preribosome in the nucleus to translation-competent 60S ribosome subunit in the cytoplasm is revealed (also see Kemmler et al. in this issue).

Cited by 108 publications

References 52 publications

Functional analysis of the uL11 protein impact on translational machinery

Functional analysis of the uL11 protein impact on translational machinery

The dual-specificity phosphatase hYVH1 (DUSP12) is a novel modulator of cellular DNA content

Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome

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