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De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

Published on: February 18, 2022

Reengineering ribosome export.

Kai-Yin Lo¹, Arlen W Johnson

¹Institute for Cellular and Molecular Biology, the University of Texas at Austin, Austin, TX 78712, USA.

Molecular Biology of the Cell

|January 16, 2009

Summary

This summary is machine-generated.

The 60S ribosomal subunit export pathway shows remarkable flexibility. Fusing different export receptors to Nmd3 enabled 60S subunit export, independent of the Crm1 receptor, suggesting adaptability in nuclear transport.

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Published on: September 29, 2012

Area of Science:

Cell Biology
Molecular Biology
Genetics

Background:

Nuclear pore complex (NPC) transport is crucial for cellular function.
Large cargoes, like the 60S ribosomal subunit, require specific export receptors.
In yeast, Crm1, Mex67/Mtr2, and Arx1 mediate 60S subunit export, but only Crm1 is conserved in higher eukaryotes.

Purpose of the Study:

To investigate whether the export of the large 60S ribosomal subunit requires a specific export receptor.
To explore the flexibility of the 60S subunit export pathway.

Main Methods:

Protein fusions were created between mutant Nmd3 and various export receptors.
The functionality of these chimeric proteins in 60S subunit export was assessed.
Experiments were conducted in the presence of the Crm1 inhibitor leptomycin B.

Main Results:

Fusions of Mex67, Los1, Mtr2, Cse1, or Msn5 to Nmd3 (lacking its NES) facilitated 60S subunit export.
This export occurred independently of Crm1, even when Crm1 was inhibited.
Directly adding a nuclear export signal (NES) to the Rpl3 protein also promoted 60S subunit export.

Conclusions:

The 60S ribosomal subunit export pathway exhibits significant flexibility, not requiring a specific receptor.
Recruitment of various export receptors can suffice for efficient 60S subunit export.
This flexibility may explain the evolution of different export receptors across eukaryotic lineages.