The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1
Most yeast ribosomal protein genes are duplicated and their characterization has led to hypotheses regarding the existence of specialized ribosomes with different subunit composition or specifically-tailored functions. In yeast, ribosomal protein genes are generally duplicated and evidence has emerg...
| Main Authors: | , , , , , , , , , , , , , , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
Public Library of Science
2013
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3750023/ |
| id |
pubmed-3750023 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-37500232013-08-29 The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 O'Leary, Monique N. Schreiber, Katherine H. Zhang, Yong Duc, Anne-Cécile E. Rao, Shuyun Hale, J. Scott Academia, Emmeline C. Shah, Shreya R. Morton, John F. Holstein, Carly A. Martin, Dan B. Kaeberlein, Matt Ladiges, Warren C. Fink, Pamela J. MacKay, Vivian L. Wiest, David L. Kennedy, Brian K. Research Article Most yeast ribosomal protein genes are duplicated and their characterization has led to hypotheses regarding the existence of specialized ribosomes with different subunit composition or specifically-tailored functions. In yeast, ribosomal protein genes are generally duplicated and evidence has emerged that paralogs might have specific roles. Unlike yeast, most mammalian ribosomal proteins are thought to be encoded by a single gene copy, raising the possibility that heterogenous populations of ribosomes are unique to yeast. Here, we examine the roles of the mammalian Rpl22, finding that Rpl22−/− mice have only subtle phenotypes with no significant translation defects. We find that in the Rpl22−/− mouse there is a compensatory increase in Rpl22-like1 (Rpl22l1) expression and incorporation into ribosomes. Consistent with the hypothesis that either ribosomal protein can support translation, knockdown of Rpl22l1 impairs growth of cells lacking Rpl22. Mechanistically, Rpl22 regulates Rpl22l1 directly by binding to an internal hairpin structure and repressing its expression. We propose that ribosome specificity may exist in mammals, providing evidence that one ribosomal protein can influence composition of the ribosome by regulating its own paralog. Public Library of Science 2013-08-22 /pmc/articles/PMC3750023/ /pubmed/23990801 http://dx.doi.org/10.1371/journal.pgen.1003708 Text en © 2013 O'Leary et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
O'Leary, Monique N. Schreiber, Katherine H. Zhang, Yong Duc, Anne-Cécile E. Rao, Shuyun Hale, J. Scott Academia, Emmeline C. Shah, Shreya R. Morton, John F. Holstein, Carly A. Martin, Dan B. Kaeberlein, Matt Ladiges, Warren C. Fink, Pamela J. MacKay, Vivian L. Wiest, David L. Kennedy, Brian K. |
| spellingShingle |
O'Leary, Monique N. Schreiber, Katherine H. Zhang, Yong Duc, Anne-Cécile E. Rao, Shuyun Hale, J. Scott Academia, Emmeline C. Shah, Shreya R. Morton, John F. Holstein, Carly A. Martin, Dan B. Kaeberlein, Matt Ladiges, Warren C. Fink, Pamela J. MacKay, Vivian L. Wiest, David L. Kennedy, Brian K. The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 |
| author_facet |
O'Leary, Monique N. Schreiber, Katherine H. Zhang, Yong Duc, Anne-Cécile E. Rao, Shuyun Hale, J. Scott Academia, Emmeline C. Shah, Shreya R. Morton, John F. Holstein, Carly A. Martin, Dan B. Kaeberlein, Matt Ladiges, Warren C. Fink, Pamela J. MacKay, Vivian L. Wiest, David L. Kennedy, Brian K. |
| author_sort |
O'Leary, Monique N. |
| title |
The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 |
| title_short |
The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 |
| title_full |
The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 |
| title_fullStr |
The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 |
| title_full_unstemmed |
The Ribosomal Protein Rpl22 Controls Ribosome Composition by Directly Repressing Expression of Its Own Paralog, Rpl22l1 |
| title_sort |
ribosomal protein rpl22 controls ribosome composition by directly repressing expression of its own paralog, rpl22l1 |
| description |
Most yeast ribosomal protein genes are duplicated and their characterization has led to hypotheses regarding the existence of specialized ribosomes with different subunit composition or specifically-tailored functions. In yeast, ribosomal protein genes are generally duplicated and evidence has emerged that paralogs might have specific roles. Unlike yeast, most mammalian ribosomal proteins are thought to be encoded by a single gene copy, raising the possibility that heterogenous populations of ribosomes are unique to yeast. Here, we examine the roles of the mammalian Rpl22, finding that Rpl22−/− mice have only subtle phenotypes with no significant translation defects. We find that in the Rpl22−/− mouse there is a compensatory increase in Rpl22-like1 (Rpl22l1) expression and incorporation into ribosomes. Consistent with the hypothesis that either ribosomal protein can support translation, knockdown of Rpl22l1 impairs growth of cells lacking Rpl22. Mechanistically, Rpl22 regulates Rpl22l1 directly by binding to an internal hairpin structure and repressing its expression. We propose that ribosome specificity may exist in mammals, providing evidence that one ribosomal protein can influence composition of the ribosome by regulating its own paralog. |
| publisher |
Public Library of Science |
| publishDate |
2013 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3750023/ |
| _version_ |
1612004943142584320 |