scholarly journals Dcm‐mediated cytosine DNA methylation is conserved in Escherichia coli and influences the expression of ribosomal protein genes

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Kevin Thomas Militello ◽  
Robert D Simon ◽  
Mehr Qureshi ◽  
Robert Maines ◽  
Michelle L VanHorne ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Methylation ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes

scholarly journals The yeast omnipotent suppressor SUP46 encodes a ribosomal protein which is a functional and structural homolog of the Escherichia coli S4 ram protein.

Genetics ◽  
1992 ◽  
Vol 132 (2) ◽  
pp. 375-386 ◽  
Author(s):  
A Vincent ◽  
S W Liebman
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Dna Sequences ◽  
Ribosomal Proteins ◽  
Amino Acid Sequences ◽  
Ribosomal Protein Genes ◽  
Significant Homology ◽  
A Cell ◽  
Functional Equivalent ◽  
Ribosomal Protein S13

Abstract The accurate synthesis of proteins is crucial to the existence of a cell. In yeast, several genes that affect the fidelity of translation have been identified (e.g., omnipotent suppressors, antisuppressors and allosuppressors). We have found that the dominant omnipotent suppressor SUP46 encodes the yeast ribosomal protein S13. S13 is encoded by two similar genes, but only the sup46 copy of the gene is able to fully complement the recessive phenotypes of SUP46 mutations. Both copies of the S13 genes contain introns. Unlike the introns of other duplicated ribosomal protein genes which are highly diverged, the duplicated S13 genes have two nearly identical DNA sequences of 25 and 31 bp in length within their introns. The SUP46 protein has significant homology to the S4 ribosomal protein in prokaryotic-type ribosomes. S4 is encoded by one of the ram (ribosomal ambiguity) genes in Escherichia coli which are the functional equivalent of omnipotent suppressors in yeast. Thus, SUP46 and S4 demonstrate functional as well as sequence conservation between prokaryotic and eukaryotic ribosomal proteins. SUP46 and S4 are most similar in their central amino acid sequences. Interestingly, the alterations resulting from the SUP46 mutations and the segment of the S4 protein involved in binding to the 16S rRNA are within this most conserved region.

Regulation of the expression of ribosomal protein genes in Escherichia coli

1975 ◽  
Vol 97 (1) ◽  
pp. 61-76 ◽  
Author(s):  
Patrick P. Dennis ◽  
Masayasu Nomura
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes

Organization of ribosomal protein genes in Escherichia coli

1976 ◽  
Vol 106 (3) ◽  
pp. 817-835 ◽  
Author(s):  
M. Fiandt ◽  
W. Szybalski ◽  
F.R. Blattner ◽  
S.R. Jaskunas ◽  
L. Lindahl ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes

Expression of ribosomal protein genes in Escherichia coli

1975 ◽  
Vol 137 (2) ◽  
pp. 125-129 ◽  
Author(s):  
Teresa Cabezón ◽  
Michel Faelen ◽  
Michel De Wilde ◽  
Alex Bollen ◽  
René Thomas
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes

scholarly journals Coexpression of Escherichia coli obgE, Encoding the Evolutionarily Conserved Obg GTPase, with Ribosomal Proteins L21 and L27

2016 ◽  
Vol 198 (13) ◽  
pp. 1857-1867 ◽  
Author(s):  
Rim Maouche ◽  
Hector L. Burgos ◽  
Laetitia My ◽  
Julie P. Viala ◽  
Richard L. Gourse ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Transcription Initiation ◽  
Ribosomal Proteins ◽  
Ribosomal Gene ◽  
Small Gtpases ◽  
Ribosomal Protein Genes ◽  
Transcriptional Terminator ◽  
Content Type

ABSTRACTMultiple essential small GTPases are involved in the assembly of the ribosome or in the control of its activity. Among them, ObgE (CgtA) has been shown recently to act as a ribosome antiassociation factor that binds to ppGpp, a regulator whose best-known target is RNA polymerase. The present study was aimed at elucidating the expression ofobgEinEscherichia coli. We show thatobgEis cotranscribed with ribosomal protein genesrplUandrpmAand with a gene of unknown function,yhbE. We show here that about 75% of the transcripts terminate beforeobgE, because there is a transcriptional terminator betweenrpmAandyhbE. As expected for ribosomal protein operons, expression was highest during exponential growth, decreased during entry into stationary phase, and became almost undetectable thereafter. Expression of the operon was derepressed in mutants lacking ppGpp or DksA. However, regulation by these factors appears to occur post-transcription initiation, since no effects of ppGpp and DksA onrplUpromoter activity were observedin vitro.IMPORTANCEThe conserved and essential ObgE GTPase binds to the ribosome and affects its assembly. ObgE has also been reported to impact chromosome segregation, cell division, resistance to DNA damage, and, perhaps most interestingly, persister formation and antibiotic tolerance. However, it is unclear whether these effects are related to its role in ribosome formation. Despite its importance, no studies on ObgE expression have been reported. We demonstrate here thatobgEis expressed from an operon encoding two ribosomal proteins, that the operon's expression varies with the growth phase, and that it is dependent on the transcription regulators ppGpp and DksA. Our results thus demonstrate thatobgEexpression is coupled to ribosomal gene expression.

Organization of ribosomal protein genes in Escherichia coli

1976 ◽  
Vol 106 (3) ◽  
pp. 837-855 ◽  
Author(s):  
Lasse Lindahl ◽  
Janice Zengel ◽  
Masayasu Nomura
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes

Phage Mu-1 mediated transposition: A tool to study the organization of ribosomal protein genes in Escherichia coli

1978 ◽  
Vol 161 (3) ◽  
pp. 291-296 ◽  
Author(s):  
Teresa Cabezón ◽  
Frédérique Van Gijsegem ◽  
Ariane Toussaint ◽  
Michel Faelen ◽  
Alex Bollen
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes ◽  
Phage Mu
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