A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq

The SMc01113/YbeY protein, belonging to the UPF0054 family, is highly conserved in nearly every bacterium. However, the function of these proteins still remains elusive. Our results show that SMc01113/YbeY proteins share structural similarities with the MID domain of the Argonaute (AGO) proteins, an...

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Main Authors: Pandey, Shree P., Minesinger, Brenda, Kumar, Janesh, Walker, Graham C.
Other Authors: Massachusetts Institute of Technology. Department of Biology
Format: Article
Language:en_US
Published: Oxford University Press 2012
Online Access:http://hdl.handle.net/1721.1/72961
https://orcid.org/0000-0001-7243-8261
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author Pandey, Shree P.
Minesinger, Brenda
Kumar, Janesh
Walker, Graham C.
author2 Massachusetts Institute of Technology. Department of Biology
author_facet Massachusetts Institute of Technology. Department of Biology
Pandey, Shree P.
Minesinger, Brenda
Kumar, Janesh
Walker, Graham C.
author_sort Pandey, Shree P.
collection MIT
description The SMc01113/YbeY protein, belonging to the UPF0054 family, is highly conserved in nearly every bacterium. However, the function of these proteins still remains elusive. Our results show that SMc01113/YbeY proteins share structural similarities with the MID domain of the Argonaute (AGO) proteins, and might similarly bind to a small-RNA (sRNA) seed, making a special interaction with the phosphate on the 5′-side of the seed, suggesting they may form a component of the bacterial sRNA pathway. Indeed, eliminating SMc01113/YbeY expression in Sinorhizobium meliloti produces symbiotic and physiological phenotypes strikingly similar to those of the hfq mutant. Hfq, an RNA chaperone, is central to bacterial sRNA-pathway. We evaluated the expression of 13 target genes in the smc01113 and hfq mutants. Further, we predicted the sRNAs that may potentially target these genes, and evaluated the accumulation of nine sRNAs in WT and smc01113 and hfq mutants. Similar to hfq, smc01113 regulates the accumulation of sRNAs as well as the target mRNAs. AGOs are central components of the eukaryotic sRNA machinery and conceptual parallels between the prokaryotic and eukaryotic sRNA pathways have long been drawn. Our study provides the first line of evidence for such conceptual parallels. Furthermore, our investigation gives insights into the sRNA-mediated regulation of stress adaptation in S. meliloti.
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spelling mit-1721.1/729612022-10-01T12:24:32Z A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq Pandey, Shree P. Minesinger, Brenda Kumar, Janesh Walker, Graham C. Massachusetts Institute of Technology. Department of Biology Walker, Graham C. Minesinger, Brenda Pandey, Shree P. Walker, Graham C. The SMc01113/YbeY protein, belonging to the UPF0054 family, is highly conserved in nearly every bacterium. However, the function of these proteins still remains elusive. Our results show that SMc01113/YbeY proteins share structural similarities with the MID domain of the Argonaute (AGO) proteins, and might similarly bind to a small-RNA (sRNA) seed, making a special interaction with the phosphate on the 5′-side of the seed, suggesting they may form a component of the bacterial sRNA pathway. Indeed, eliminating SMc01113/YbeY expression in Sinorhizobium meliloti produces symbiotic and physiological phenotypes strikingly similar to those of the hfq mutant. Hfq, an RNA chaperone, is central to bacterial sRNA-pathway. We evaluated the expression of 13 target genes in the smc01113 and hfq mutants. Further, we predicted the sRNAs that may potentially target these genes, and evaluated the accumulation of nine sRNAs in WT and smc01113 and hfq mutants. Similar to hfq, smc01113 regulates the accumulation of sRNAs as well as the target mRNAs. AGOs are central components of the eukaryotic sRNA machinery and conceptual parallels between the prokaryotic and eukaryotic sRNA pathways have long been drawn. Our study provides the first line of evidence for such conceptual parallels. Furthermore, our investigation gives insights into the sRNA-mediated regulation of stress adaptation in S. meliloti. National Institutes of Health (U.S.) (grant GM31030) Massachusetts Institute of Technology. Center for Environmental Health Sciences (NIEHS P30 ES002109) National Institutes of Health (U.S.) (fellowship F32 GM078966) 2012-09-14T15:47:06Z 2012-09-14T15:47:06Z 2011-02 2011-01 Article http://purl.org/eprint/type/JournalArticle 0305-1048 1362-4962 http://hdl.handle.net/1721.1/72961 Pandey, S. P. et al. “A Highly Conserved Protein of Unknown Function in Sinorhizobium Meliloti Affects sRNA Regulation Similar to Hfq.” Nucleic Acids Research 39.11 (2011): 4691–4708. Web. https://orcid.org/0000-0001-7243-8261 en_US http://dx.doi.org/10.1093/nar/gkr060 Nucleic Acids Research Creative Commons Attribution Non-Commercial http://creativecommons.org/licenses/by-nc/2.5 application/pdf Oxford University Press Oxford
spellingShingle Pandey, Shree P.
Minesinger, Brenda
Kumar, Janesh
Walker, Graham C.
A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
title A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
title_full A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
title_fullStr A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
title_full_unstemmed A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
title_short A highly conserved protein of unknown function in Sinorhizobium meliloti affects sRNA regulation similar to Hfq
title_sort highly conserved protein of unknown function in sinorhizobium meliloti affects srna regulation similar to hfq
url http://hdl.handle.net/1721.1/72961
https://orcid.org/0000-0001-7243-8261
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