Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome

Nature Communications
Yi ZhouDavid W Taylor

Abstract

The catalytic activity of the ribosome is mediated by RNA, yet proteins are essential for the function of the peptidyl transferase center (PTC). In eukaryotes, final assembly of the PTC occurs in the cytoplasm by insertion of the ribosomal protein Rpl10 (uL16). We determine structures of six intermediates in late nuclear and cytoplasmic maturation of the large subunit that reveal a tightly-choreographed sequence of protein and RNA rearrangements controlling the insertion of Rpl10. We also determine the structure of the biogenesis factor Yvh1 and show how it promotes assembly of the P stalk, a critical element for recruitment of GTPases that drive translation. Together, our structures provide a blueprint for final assembly of a functional ribosome.

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Citations

May 23, 2019·ELife·Vasileios KargasAlan John Warren
Nov 11, 2019·Biomolecules·Michael PrattesRobin E Stanley
May 5, 2020·Nucleic Acids Research·Miriam OlombradaVikram Govind Panse
Jul 17, 2020·Frontiers in Plant Science·Federico Martinez-SeidelJoachim Kopka
Jun 6, 2019·International Journal of Molecular Sciences·Manuela PiazziWilliam L Blalock
Aug 28, 2020·The Journal of Biological Chemistry·Ying XieYansong Miao
Dec 4, 2020·International Journal of Molecular Sciences·Helge PaternogaEd Hurt
Nov 25, 2020·Cells·Daniela Pollutri, Marianna Penzo
Jul 3, 2021·International Journal of Molecular Sciences·Federico Martinez-SeidelAlexandre Augusto Pereira Firmino

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Methods Mentioned

BETA
GTPase
GTPases
tandem affinity purification
protein exchanges
PCR
affinity purification

Software Mentioned

Segger
Coot
MSI
Chimera
MotionCor2
UCSF Chimera
RELION
LEGINON
Appion
PyMOL

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