The Extended Loops of Ribosomal Proteins L4 and L22 Are Not Required for Ribosome Assembly or L4-mediated Autogenous Control

Overview

Journal RNA

Specialty Molecular Biology

Date 2003 Sep 18

PMID 13130133

Citations 28

Authors

Janice M Zengel

Adam Jerauld

Andre Walker

Markus C Wahl

Lasse Lindahl

Affiliations

Soon will be listed here.

Abstract

Ribosomal proteins L4 and L22 both have a globular domain that sits on the surface of the large ribosomal subunit and an extended loop that penetrates its core. The tips of both loops contribute to the lining of the peptide exit tunnel and have been implicated in a gating mechanism that might regulate the exit of nascent peptides. Also, the extensions of L4 and L22 contact multiple domains of 23S rRNA, suggesting they might facilitate rRNA folding during ribosome assembly. To learn more about the roles of these extensions, we constructed derivatives of both proteins that lack most of their extended loops. Our analysis of ribosomes carrying L4 or L22 deletion proteins did not detect any significant difference in their sedimentation property or polysome distribution. Also, the role of L4 in autogenous control was not affected. We conclude that these extensions are not required for ribosome assembly or for L4-mediated autogenous control of the S10 operon.

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