Limited Role for the DsrA and RprA Regulatory RNAs in rpoS Regulation in Salmonella enterica
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Published in | Journal of Bacteriology Vol. 188; no. 14; pp. 5077 - 5088 |
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01.07.2006
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ISSN | 0021-9193 1067-8832 1098-5530 |
DOI | 10.1128/JB.00206-06 |
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RpoS, the sigma factor of enteric bacteria that responds to stress and stationary phase, is subject to complex regulation acting at multiple levels, including transcription, translation, and proteolysis. Increased translation of rpoS mRNA during growth at low temperature, after osmotic challenge, or with a constitutively activated Rcs phosphorelay depends on two trans -acting small regulatory RNAs (sRNAs) in Escherichia coli . The DsrA and RprA sRNAs are both highly conserved in Salmonella enterica , as is their target, an inhibitory antisense element within the rpoS untranslated leader. Analysis of dsrA and rprA deletion mutants indicates that while the increased translation of RpoS in response to osmotic challenge is conserved in S. enterica , dependence on these two sRNA regulators is much reduced. Furthermore, low-temperature growth or constitutive RcsC activation had only modest effects on RpoS expression, and these increases were, respectively, independent of dsrA or rprA function. This lack of conservation of sRNA function suggests surprising flexibility in RpoS regulation. RpoS, the sigma factor of enteric bacteria that responds to stress and stationary phase, is subject to complex regulation acting at multiple levels, including transcription, translation, and proteolysis. Increased translation of rpoS mRNA during growth at low temperature, after osmotic challenge, or with a constitutively activated Rcs phosphorelay depends on two trans-acting small regulatory RNAs (sRNAs) in Escherichia coli. The DsrA and RprA sRNAs are both highly conserved in Salmonella enterica, as is their target, an inhibitory antisense element within the rpoS untranslated leader. Analysis of dsrA and rprA deletion mutants indicates that while the increased translation of RpoS in response to osmotic challenge is conserved in S. enterica, dependence on these two sRNA regulators is much reduced. Furthermore, low-temperature growth or constitutive RcsC activation had only modest effects on RpoS expression, and these increases were, respectively, independent of dsrA or rprA function. This lack of conservation of sRNA function suggests surprising flexibility in RpoS regulation. RpoS, the sigma factor of enteric bacteria that responds to stress and stationary phase, is subject to complex regulation acting at multiple levels, including transcription, translation, and proteolysis. Increased translation of rpoS mRN during growth at low temperature, after osmotic challenge, or with a constitutively activated Rcs phosphorelay depends on two trans-acting small regulatory RNAs (sRNAs) in Escherichia coli. The DsrA and RprA sRNAs are both highly conserved in Salmonella enterica, as is their target, an inhibitory antisense element within the rpoS untranslated leader. Analysis of dsrA and rprA deletion mutants indicates that while the increased translation of RpoS in response to osmotic challenge is conserved in S. enterica, dependence on these two sRNA regulators is much reduced. Furthermore, low-temperature growth or constitutive RcsC activation had only modest effects on RpoS expression, and these increases were, respectively, independent of dsrA or rprA function. This lack of conservation of sRNA function suggests surprising flexibility in RpoS regulation. [PUBLICATION ABSTRACT] RpoS, the sigma factor of enteric bacteria that responds to stress and stationary phase, is subject to complex regulation acting at multiple levels, including transcription, translation, and proteolysis. Increased translation of rpoS mRNA during growth at low temperature, after osmotic challenge, or with a constitutively activated Rcs phosphorelay depends on two trans-acting small regulatory RNAs (sRNAs) in Escherichia coli. The DsrA and RprA sRNAs are both highly conserved in Salmonella enterica, as is their target, an inhibitory antisense element within the rpoS untranslated leader. Analysis of dsrA and rprA deletion mutants indicates that while the increased translation of RpoS in response to osmotic challenge is conserved in S. enterica, dependence on these two sRNA regulators is much reduced. Furthermore, low-temperature growth or constitutive RcsC activation had only modest effects on RpoS expression, and these increases were, respectively, independent of dsrA or rprA function. This lack of conservation of sRNA function suggests surprising flexibility in RpoS regulation.RpoS, the sigma factor of enteric bacteria that responds to stress and stationary phase, is subject to complex regulation acting at multiple levels, including transcription, translation, and proteolysis. Increased translation of rpoS mRNA during growth at low temperature, after osmotic challenge, or with a constitutively activated Rcs phosphorelay depends on two trans-acting small regulatory RNAs (sRNAs) in Escherichia coli. The DsrA and RprA sRNAs are both highly conserved in Salmonella enterica, as is their target, an inhibitory antisense element within the rpoS untranslated leader. Analysis of dsrA and rprA deletion mutants indicates that while the increased translation of RpoS in response to osmotic challenge is conserved in S. enterica, dependence on these two sRNA regulators is much reduced. Furthermore, low-temperature growth or constitutive RcsC activation had only modest effects on RpoS expression, and these increases were, respectively, independent of dsrA or rprA function. This lack of conservation of sRNA function suggests surprising flexibility in RpoS regulation. |
Author | Thomas Elliott Amy M. Jones Adam Goodwill |
AuthorAffiliation | Department of Microbiology, Immunology and Cell Biology, West Virginia University Health Sciences Center, Morgantown, West Virginia 26506 |
AuthorAffiliation_xml | – name: Department of Microbiology, Immunology and Cell Biology, West Virginia University Health Sciences Center, Morgantown, West Virginia 26506 |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16816180$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1128_ecosal_2_4_2_2 crossref_primary_10_1093_nar_gkp646 crossref_primary_10_1128_aem_02158_23 crossref_primary_10_1093_nar_gkt148 crossref_primary_10_1128_JB_00659_20 crossref_primary_10_1371_journal_pgen_1000163 crossref_primary_10_1016_j_biochi_2017_03_005 crossref_primary_10_1073_pnas_1507825112 crossref_primary_10_1016_j_mib_2010_01_001 crossref_primary_10_2217_fmb_10_83 crossref_primary_10_4161_rna_20480 crossref_primary_10_1016_j_ijfoodmicro_2016_06_022 crossref_primary_10_1016_j_foodres_2011_06_056 crossref_primary_10_1111_mmi_12011 crossref_primary_10_1111_j_1365_2958_2008_06505_x crossref_primary_10_1016_j_ddmec_2010_09_001 crossref_primary_10_1111_j_1365_2958_2006_05489_x crossref_primary_10_1371_journal_pone_0072527 crossref_primary_10_1021_pr101294v crossref_primary_10_1099_mic_0_033936_0 crossref_primary_10_1261_rna_603108 crossref_primary_10_1093_nar_gkm916 crossref_primary_10_4161_rna_19682 |
Cites_doi | 10.1128/jb.143.2.926-933.1980 10.1128/jb.178.13.3763-3770.1996 10.1046/j.1365-2958.2003.03454.x 10.1073/pnas.95.21.12462 10.1128/MMBR.66.3.373-395.2002 10.1128/jb.119.3.736-747.1974 10.1073/pnas.96.11.6439 10.1101/gad.901001 10.1016/S0378-1119(02)00551-6 10.1128/JB.185.8.2673-2679.2003 10.1128/JB.183.6.1997-2005.2001 10.1073/pnas.170281497 10.1128/JB.184.18.5077-5087.2002 10.1128/JB.183.13.4012-4023.2001 10.1128/jb.173.13.4144-4154.1991 10.1128/JB.184.12.3167-3175.2002 10.1002/j.1460-2075.1996.tb00773.x 10.1111/j.1365-2958.1995.mmi_17010155.x 10.1128/jb.179.3.656-662.1997 10.1128/JB.185.22.6609-6614.2003 10.1128/JB.183.19.5782-5787.2001 10.1128/JB.186.18.6179-6185.2004 10.1128/jb.177.14.4121-4130.1995 10.1101/gad.10.9.1143 10.1128/JB.183.20.5974-5981.2001 10.1128/iai.65.1.203-210.1997 10.1128/jb.145.2.1110-1111.1981 10.1046/j.1365-2958.2002.03203.x 10.1099/mic.0.27520-0 10.1016/S0021-9258(18)34138-3 10.1128/JB.187.5.1568-1580.2005 10.1093/genetics/119.1.9 10.1093/emboj/17.20.6061 10.1128/iai.64.6.2365-2367.1996 10.1128/JB.181.16.4853-4862.1999 10.1111/j.1365-2958.2001.02329.x 10.1073/pnas.100127597 10.1128/JB.180.17.4564-4570.1998 10.1073/pnas.120163297 10.1146/annurev.micro.58.030603.123841 10.1016/0378-1119(95)00793-8 10.1128/JB.187.5.1591-1603.2005 10.1080/10409230590918702 10.1007/BF00284200 10.1046/j.1365-2958.1999.01581.x 10.1073/pnas.92.6.2003 10.1128/jb.177.16.4676-4680.1995 10.1128/jb.158.2.488-495.1984 |
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Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 Corresponding author. Mailing address: Department of Microbiology, Immunology and Cell Biology, West Virginia University Health Sciences Center, Morgantown, WV 26506. Phone: (304) 293-2676. Fax: (304) 293-7823. E-mail: telliott@hsc.wvu.edu. |
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Mendeley... RpoS, the sigma factor of enteric bacteria that responds to stress and stationary phase, is subject to complex regulation acting at multiple levels, including... |
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SubjectTerms | Bacteria Bacterial Proteins - genetics Bacteriology Base Sequence Conserved Sequence E coli Escherichia coli Gene Expression Regulation, Bacterial Gene Regulation Kinetics Low temperature Molecular Sequence Data Nucleic Acid Conformation Ribonucleic acid RNA RNA, Antisense - chemistry RNA, Antisense - genetics RNA, Bacterial - chemistry RNA, Bacterial - genetics RNA, Small Cytoplasmic - chemistry RNA, Small Cytoplasmic - genetics RNA, Small Untranslated RNA, Untranslated - chemistry RNA, Untranslated - genetics Salmonella enterica Salmonella enterica - genetics Salmonella enterica - growth & development Sigma Factor - genetics Temperature |
Title | Limited Role for the DsrA and RprA Regulatory RNAs in rpoS Regulation in Salmonella enterica |
URI | http://jb.asm.org/content/188/14/5077.abstract https://www.ncbi.nlm.nih.gov/pubmed/16816180 https://www.proquest.com/docview/227102159 https://www.proquest.com/docview/17264582 https://www.proquest.com/docview/68593947 https://pubmed.ncbi.nlm.nih.gov/PMC1539969 |
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