Mapping of the genes for Bacillus subtilis ribosomal proteins S6 and S16: Comparison of the chromosomal distribution of ribosomal protein genes in this bacterium with the distribution in Escherichia coli

1983 ◽  
Vol 192 (3) ◽  
pp. 386-390 ◽  
Author(s):  
Eric R. Dabbs
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Ribosomal Protein Genes ◽  
Chromosomal Distribution

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.

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.

Regulation of the Escherichia coli S10 ribosomal protein operon by heterologous L4 ribosomal proteins

1995 ◽  
Vol 73 (11-12) ◽  
pp. 1105-1112 ◽  
Author(s):  
Janice M. Zengel ◽  
Dariya Vorozheikina ◽  
Xiao Li ◽  
Lasse Lindahl
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Yersinia Pseudotuberculosis ◽  
Bacillus Stearothermophilus ◽  
Ribosomal Protein Genes ◽  
Haemophilus Influenza ◽  
E Coli ◽  
Autogenous Control ◽  
Ribosomal Protein Operon

We have cloned the L4 ribosomal protein genes from Morganella morganii and Haemophilus influenza. The sequences of these genes were compared with published sequences for Escherichia coli, Yersinia pseudotuberculosis, and Bacillus stearothermophilus. All five of these L4 genes were expressed in E. coli and shown to function as repressors of both transcription and translation of the E. coli S10 operon. Possible implications for regulation of r-protein synthesis in species other than E. coli are discussed.Key words: ribosomes, autogenous control, r-protein L4, phylogeny.

Comparative studies of ribosomal proteins and their genes from Methanococcus vannielii and other organisms

1989 ◽  
Vol 35 (1) ◽  
pp. 11-20 ◽  
Author(s):  
Andreas K. E. Köpke ◽  
Brigitte Wittmann-Liebold
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Methanogenic Bacteria ◽  
Gene Organization ◽  
Amino Acid Sequences ◽  
Ribosomal Protein Genes ◽  
Protein Sequence Analysis ◽  
Protein Coding ◽  
Using Data

Using data from a partial protein sequence analysis of ribosomal proteins derived from the archaebacterium Methanococcus vannielii, oligonucleotide probes were synthesized. The probes enabled us to localize several ribosomal protein genes and to determine their nucleotide sequences. The amino acid sequences that were deduced from the genes correspond to proteins L12 and L10 from the rif operon, according to the genome organization in Escherichia coli, and to proteins L23 and L2, which have comparable locations, as in the Escherichia coli S10 operon. Various degrees of similarity were found when the four proteins were compared with the corresponding ribosomal proteins of prokaryotic or eukaryotic organisms. The highest sequence homology was found in counterparts from other archaebacteria, such as Halobacterium marismortui, Halobacterium halobium, or Sulfolobus. In general, the M. vannielii protein sequences were more related to the eukaryotic kingdom than to the Gram-positive or Gram-negative eubacteria. On the other hand, the organization of the ribosomal protein genes clearly follows the operon structure of the Escherichia coli genome and is different from the monocistronic eukaryotic gene arrangements. The protein coding regions were not interrupted by introns. Furthermore, the Shine–Dalgarno type sequences of methanogenic bacteria are homologous with those of eubacteria, and also their terminator regions are similar.Key words: archaebacteria, ribosomal proteins, evolution, gene organization, Methanococcus vannielii.

Mild temperature shock alters the transcription of a discrete class of Saccharomyces cerevisiae genes

1983 ◽  
Vol 3 (3) ◽  
pp. 457-465
Author(s):  
C H Kim ◽  
J R Warner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Temperature Shift ◽  
Restrictive Temperature ◽  
Ribosomal Protein Genes ◽  
Wild Type ◽  
Temperature Shock ◽  
Mild Temperature ◽  
Mutant Cells

In Saccharomyces cerevisiae the synthesis of ribosomal proteins declines temporarily after a culture has been subjected to a mild temperature shock, i.e., a shift from 23 to 36 degrees C, each of which support growth. Using cloned genes for several S. cerevisiae ribosomal proteins, we found that the changes in the synthesis of ribosomal proteins parallel the changes in the concentration of mRNA of each. The disappearance and reappearance of the mRNA is due to a brief but severe inhibition of the transcription of each of the ribosomal protein genes, although the total transcription of mRNA in the cells is relatively unaffected by the temperature shock. The precisely coordinated response of these genes, which are scattered throughout the genome, suggests that either they or the enzyme which transcribes them has unique properties. In certain S. cerevisiae mutants, the synthesis of ribosomal proteins never recovers from a temperature shift. Yet both the decline and the resumption of transcription of these genes during the 30 min after the temperature shift are indistinguishable from those in wild-type cells. The failure of the mutant cells to grow at the restrictive temperature appears to be due to their inability to process the RNA transcribed from genes which have introns (Rosbash et al., Cell 24:679-686, 1981), a large proportion of which appear to be ribosomal protein genes.

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 Inactivation of Ribosomal Protein Genes in Bacillus subtilis Reveals Importance of Each Ribosomal Protein for Cell Proliferation and Cell Differentiation

2012 ◽  
Vol 194 (22) ◽  
pp. 6282-6291 ◽  
Author(s):  
G. Akanuma ◽  
H. Nanamiya ◽  
Y. Natori ◽  
K. Yano ◽  
S. Suzuki ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Bacillus Subtilis ◽  
Cell Differentiation ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes
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