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The CRM domain: An RNA binding module derived from an ancient ribosome-associated protein
Year:
2007
Source of publication :
Authors :
Ostersetzer, Oren
;
.
Volume :
13
Co-Authors:
Barkan, A., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Klipcan, L., Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Ostersetzer, O., Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Kawamura, T., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States, Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, CA 93106-9510, United States
Asakura, Y., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States
Watkins, K.P., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States
Facilitators :
From page:
55
To page:
64
(
Total pages:
10
)
Abstract:
The CRS1-YhbY domain (also called the CRM domain) is represented as a stand-alone protein in Archaea and Bacteria, and in a family of single- and multidomain proteins in plants. The function of this domain is unknown, but structural data and the presence of the domain in several proteins known to interact with RNA have led to the proposal that it binds RNA. Here we describe a phylogenetic analysis of the domain, its incorporation into diverse proteins in plants, and biochemical properties of a prokaryotic and eukaryotic representative of the domain family. We show that a bacterial member of the family, Escherichia coli YhbY, is associated with pre-50S ribosomal subunits, suggesting that YhbY functions in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. We show further that an isolated maize CRM domain has RNA binding activity in vitro, and that a small motif shared with KH RNA binding domains, a conserved "GxxG" loop, contributes to its RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 RNA Society.
Note:
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More details
DOI :
10.1261/rna.139607
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19696
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:30
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Scientific Publication
The CRM domain: An RNA binding module derived from an ancient ribosome-associated protein
13
Barkan, A., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Klipcan, L., Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Ostersetzer, O., Agricultural Research Organization, Volcani Center, Bet Dagan 50250, Israel
Kawamura, T., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States, Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, CA 93106-9510, United States
Asakura, Y., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States
Watkins, K.P., Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, United States
The CRM domain: An RNA binding module derived from an ancient ribosome-associated protein
The CRS1-YhbY domain (also called the CRM domain) is represented as a stand-alone protein in Archaea and Bacteria, and in a family of single- and multidomain proteins in plants. The function of this domain is unknown, but structural data and the presence of the domain in several proteins known to interact with RNA have led to the proposal that it binds RNA. Here we describe a phylogenetic analysis of the domain, its incorporation into diverse proteins in plants, and biochemical properties of a prokaryotic and eukaryotic representative of the domain family. We show that a bacterial member of the family, Escherichia coli YhbY, is associated with pre-50S ribosomal subunits, suggesting that YhbY functions in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. We show further that an isolated maize CRM domain has RNA binding activity in vitro, and that a small motif shared with KH RNA binding domains, a conserved "GxxG" loop, contributes to its RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 RNA Society.
Scientific Publication
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