A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit

A comparison of overlapping proximity captures at the head region of the ribosomal 40S subunit (<i>hr40S</i>) in <i>Saccharomyces cerevisiae</i> from four adjacent perspectives, namely Asc1/RACK1, Rps2/uS5, Rps3/uS3, and Rps20/uS10, corroborates dynamic co-localization of pro...

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Autores principales:	Kerstin Schmitt, Alina-Andrea Kraft, Oliver Valerius
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	biotin identification (BioID) Asc1/RACK1 Rps2/uS5 Rps3/uS3 Rps20/uS10 Rpl5/uL18 Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/11c9f7cf9fb5463da80a24fddbe46e91
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spelling	oai:doaj.org-article:11c9f7cf9fb5463da80a24fddbe46e912021-11-11T17:07:36ZA Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit10.3390/ijms2221116531422-00671661-6596https://doaj.org/article/11c9f7cf9fb5463da80a24fddbe46e912021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11653https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067A comparison of overlapping proximity captures at the head region of the ribosomal 40S subunit (<i>hr40S</i>) in <i>Saccharomyces cerevisiae</i> from four adjacent perspectives, namely Asc1/RACK1, Rps2/uS5, Rps3/uS3, and Rps20/uS10, corroborates dynamic co-localization of proteins that control activity and fate of both ribosomes and mRNA. Co-locating factors that associate with the <i>hr40S</i> are involved in (i) (de)ubiquitination of ribosomal proteins (Hel2, Bre5-Ubp3), (ii) clamping of inactive ribosomal subunits (Stm1), (iii) mRNA surveillance and vesicular transport (Smy2, Syh1), (iv) degradation of mRNA (endo- and exonucleases Ypl199c and Xrn1, respectively), (v) autophagy (Psp2, Vps30, Ykt6), and (vi) kinase signaling (Ste20). Additionally, they must be harmonized with translation initiation factors (eIF3, cap-binding protein Cdc33, eIF2A) and mRNA-binding/ribosome-charging proteins (Scp160, Sro9). The Rps/uS-BioID perspectives revealed substantial Asc1/RACK1-dependent <i>hr40S</i> configuration indicating a function of the β-propeller in context-specific spatial organization of this microenvironment. Toward resolving context-specific constellations, a Split-TurboID analysis emphasized the ubiquitin-associated factors Def1 and Lsm12 as neighbors of Bre5 at <i>hr40S</i>. These shuttling proteins indicate a common regulatory axis for the fate of polymerizing machineries for the biosynthesis of proteins in the cytoplasm and RNA/DNA in the nucleus.Kerstin SchmittAlina-Andrea KraftOliver ValeriusMDPI AGarticlebiotin identification (BioID)Asc1/RACK1Rps2/uS5Rps3/uS3Rps20/uS10Rpl5/uL18Biology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11653, p 11653 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	biotin identification (BioID) Asc1/RACK1 Rps2/uS5 Rps3/uS3 Rps20/uS10 Rpl5/uL18 Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	biotin identification (BioID) Asc1/RACK1 Rps2/uS5 Rps3/uS3 Rps20/uS10 Rpl5/uL18 Biology (General) QH301-705.5 Chemistry QD1-999 Kerstin Schmitt Alina-Andrea Kraft Oliver Valerius A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit
description	A comparison of overlapping proximity captures at the head region of the ribosomal 40S subunit (<i>hr40S</i>) in <i>Saccharomyces cerevisiae</i> from four adjacent perspectives, namely Asc1/RACK1, Rps2/uS5, Rps3/uS3, and Rps20/uS10, corroborates dynamic co-localization of proteins that control activity and fate of both ribosomes and mRNA. Co-locating factors that associate with the <i>hr40S</i> are involved in (i) (de)ubiquitination of ribosomal proteins (Hel2, Bre5-Ubp3), (ii) clamping of inactive ribosomal subunits (Stm1), (iii) mRNA surveillance and vesicular transport (Smy2, Syh1), (iv) degradation of mRNA (endo- and exonucleases Ypl199c and Xrn1, respectively), (v) autophagy (Psp2, Vps30, Ykt6), and (vi) kinase signaling (Ste20). Additionally, they must be harmonized with translation initiation factors (eIF3, cap-binding protein Cdc33, eIF2A) and mRNA-binding/ribosome-charging proteins (Scp160, Sro9). The Rps/uS-BioID perspectives revealed substantial Asc1/RACK1-dependent <i>hr40S</i> configuration indicating a function of the β-propeller in context-specific spatial organization of this microenvironment. Toward resolving context-specific constellations, a Split-TurboID analysis emphasized the ubiquitin-associated factors Def1 and Lsm12 as neighbors of Bre5 at <i>hr40S</i>. These shuttling proteins indicate a common regulatory axis for the fate of polymerizing machineries for the biosynthesis of proteins in the cytoplasm and RNA/DNA in the nucleus.
format	article
author	Kerstin Schmitt Alina-Andrea Kraft Oliver Valerius
author_facet	Kerstin Schmitt Alina-Andrea Kraft Oliver Valerius
author_sort	Kerstin Schmitt
title	A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit
title_short	A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit
title_full	A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit
title_fullStr	A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit
title_full_unstemmed	A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit
title_sort	multi-perspective proximity view on the dynamic head region of the ribosomal 40s subunit
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/11c9f7cf9fb5463da80a24fddbe46e91
work_keys_str_mv	AT kerstinschmitt amultiperspectiveproximityviewonthedynamicheadregionoftheribosomal40ssubunit AT alinaandreakraft amultiperspectiveproximityviewonthedynamicheadregionoftheribosomal40ssubunit AT olivervalerius amultiperspectiveproximityviewonthedynamicheadregionoftheribosomal40ssubunit AT kerstinschmitt multiperspectiveproximityviewonthedynamicheadregionoftheribosomal40ssubunit AT alinaandreakraft multiperspectiveproximityviewonthedynamicheadregionoftheribosomal40ssubunit AT olivervalerius multiperspectiveproximityviewonthedynamicheadregionoftheribosomal40ssubunit
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A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit

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