An open interface in the pre-80S ribosome coordinated by ribosome assembly factors Tsr1 and Dim1 enables temporal regulation of Fap7.

Rai, Jay; Parker, Melissa D; Huang, Haina; Choy, Stefan; Ghalei, Homa; Johnson, Matthew C; Karbstein, Katrin; Stroupe, M Elizabeth

Rai, Jay; Parker, Melissa D; Huang, Haina; Choy, Stefan; Ghalei, Homa; Johnson, Matthew C; Karbstein, Katrin; Stroupe, M Elizabeth.

Afiliación

Rai J; Department of Biological Science and the Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
Parker MD; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458, USA.
Huang H; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458, USA.
Choy S; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458, USA.
Ghalei H; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458, USA.
Johnson MC; Department of Biological Science and the Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
Karbstein K; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458, USA.
Stroupe ME; HHMI Faculty Scholar, Howard Hughes Medical Institute, Chevy Chase, Maryland 20815, USA.

RNA ; 27(2): 221-233, 2021 02.

Article en En | MEDLINE | ID: mdl-33219089

RESUMEN

During their maturation, nascent 40S subunits enter a translation-like quality control cycle, where they are joined by mature 60S subunits to form 80S-like ribosomes. While these assembly intermediates are essential for maturation and quality control, how they form, and how their structure promotes quality control, remains unknown. To address these questions, we determined the structure of an 80S-like ribosome assembly intermediate to an overall resolution of 3.4 Å. The structure, validated by biochemical data, resolves a large body of previously paradoxical data and illustrates how assembly and translation factors cooperate to promote the formation of an interface that lacks many mature subunit contacts but is stabilized by the universally conserved methyltransferase Dim1. We also show how Tsr1 enables this interface by blocking the canonical binding of eIF5B to 40S subunits, while maintaining its binding to 60S. The structure also shows how this interface leads to unfolding of the platform, which allows for temporal regulation of the ATPase Fap7, thus linking 40S maturation to quality control during ribosome assembly.

Asunto(s)

Adenilato Quinasa/genética; Regulación Fúngica de la Expresión Génica; Metiltransferasas/genética; Proteínas Nucleares/genética; Nucleósido-Trifosfatasa/genética; Proteínas Ribosómicas/genética; Subunidades Ribosómicas Grandes de Eucariotas/genética; Subunidades Ribosómicas Pequeñas de Eucariotas/genética; Proteínas de Saccharomyces cerevisiae/genética; Saccharomyces cerevisiae/genética; Adenilato Quinasa/química; Adenilato Quinasa/metabolismo; Sitios de Unión; Metiltransferasas/química; Metiltransferasas/metabolismo; Modelos Moleculares; Proteínas Nucleares/química; Proteínas Nucleares/metabolismo; Nucleósido-Trifosfatasa/química; Nucleósido-Trifosfatasa/metabolismo; Biogénesis de Organelos; Unión Proteica; Biosíntesis de Proteínas; Conformación Proteica en Hélice alfa; Conformación Proteica en Lámina beta; Dominios y Motivos de Interacción de Proteínas; Proteínas Ribosómicas/química; Proteínas Ribosómicas/metabolismo; Subunidades Ribosómicas Grandes de Eucariotas/metabolismo; Subunidades Ribosómicas Grandes de Eucariotas/ultraestructura; Subunidades Ribosómicas Pequeñas de Eucariotas/metabolismo; Subunidades Ribosómicas Pequeñas de Eucariotas/ultraestructura; Saccharomyces cerevisiae/metabolismo; Proteínas de Saccharomyces cerevisiae/química; Proteínas de Saccharomyces cerevisiae/metabolismo

Palabras clave

cryo-EM; ribosome assembly; small ribosome subunit

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Ribosómicas / Saccharomyces cerevisiae / Proteínas Nucleares / Regulación Fúngica de la Expresión Génica / Adenilato Quinasa / Proteínas de Saccharomyces cerevisiae / Nucleósido-Trifosfatasa / Subunidades Ribosómicas Grandes de Eucariotas / Subunidades Ribosómicas Pequeñas de Eucariotas / Metiltransferasas Tipo de estudio: Prognostic_studies Idioma: En Revista: RNA Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

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