Google Scholar. Oxford University Press is a department of the University of Oxford. It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide. Sign In or Create an Account. Sign In. Advanced Search. Search Menu. Article Navigation. Close mobile search navigation Article Navigation. Volume Article Contents Abstract.
Transcription and Translation are Coupled in Archaea. French , Sarah L. Oxford Academic. Thomas J. Ann L. John N. William Martin, Associate Editor. Cite Cite Sarah L. Select Format Select format.
Permissions Icon Permissions. Abstract Polysomes have been visualized by electron microscopy attached directly to dispersed strands of genomic DNA extruded from lysed cells of the hyperthermophilic archaeon Thermococcus kodakaraensis. Archaea , prokaryote , coupled transcription , polysome , electron microscopy. Open in new tab Download slide. Description of Thermococcus kodakaraensis sp. Google Scholar Crossref.
The three dimensional shape taken by tRNAs. Each tRNA has a sequence of three nucleotides located in a loop at one end of the molecule that can basepair with an mRNA codon. Each different tRNA has a different anticodon. When the tRNA anticodon basepairs with one of the mRNA codons, the tRNA will add an amino acid to a growing polypeptide chain or terminate translation, according to the genetic code.
The tRNA with this anticodon would be linked to the amino acid leucine. The corresponding amino acid must be added later, once the tRNA is processed and exported to the cytoplasm. At least one type of aminoacyl tRNA synthetase exists for each of the 21 amino acids; the exact number of aminoacyl tRNA synthetases varies by species. These enzymes first bind and hydrolyze ATP to catalyze the formation of a covalent bond between an amino acid and adenosine monophosphate AMP ; a pyrophosphate molecule is expelled in this reaction.
The same enzyme then catalyzes the attachment of the activated amino acid to the tRNA and the simultaneous release of AMP. After the correct amino acid covalently attached to the tRNA, it is released by the enzyme. The tRNA is said to be charged with its cognate amino acid.
Prokaryotic transcription occurs in the cytoplasm alongside translation and can occur simultaneously. Prokaryotic transcription is the process in which messenger RNA transcripts of genetic material in prokaryotes are produced, to be translated for the production of proteins.
Prokaryotic transcription occurs in the cytoplasm alongside translation. Prokaryotic transcription and translation can occur simultaneously. This is impossible in eukaryotes, where transcription occurs in a membrane-bound nucleus while translation occurs outside the nucleus in the cytoplasm.
In prokaryotes genetic material is not enclosed in a membrane-enclosed nucleus and has access to ribosomes in the cytoplasm. Protein synthesis : An overview of protein synthesis.
This RNA is then subject to post-transcriptional modification and control, resulting in a mature mRNA red that is then transported out of the nucleus and into the cytoplasm peach , where it undergoes translation into a protein.
Newly synthesized proteins black are often further modified, such as by binding to an effector molecule orange , to become fully active. Transcription is controlled by a variety of regulators in prokaryotes. Many of these transcription factors are homodimers containing helix-turn-helix DNA-binding motifs. Promoter strength is in many but not all cases, a matter of how tightly RNA polymerase and its associated accessory proteins bind to their respective DNA sequences.
The more similar the sequences are to a consensus sequence, the stronger the binding is. Additional transcription regulation comes from transcription factors that can affect the stability of the holoenzyme structure at initiation. Two termination mechanisms are well known: Intrinsic termination also called Rho-independent transcription termination involves terminator sequences within the RNA that signal the RNA polymerase to stop.
The terminator sequence is usually a palindromic sequence that forms a stem-loop hairpin structure that leads to the dissociation of the RNAP from the DNA template. Aside from the 22 standard amino acids, there are many other amino acids that are called non-proteinogenic or non-standard.
Posttranslational modification PTM is the chemical modification of a protein after its translation. It is one of the later steps in protein biosynthesis, and thus gene expression, for many proteins. A protein also called a polypeptide is a chain of amino acids. During protein synthesis, 20 different amino acids can be incorporated to become a protein. After translation, the posttranslational modification of amino acids extends the range of functions of the protein by attaching it to other biochemical functional groups such as acetate, phosphate, various lipids, and carbohydrates , changing the chemical nature of an amino acid e.
Also, enzymes may remove amino acids from the amino end of the protein, or cut the peptide chain in the middle. For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by disulfide bonds. This amino acid is usually taken off during post-translational modification.
Those either are not found in proteins e. Genetic code : The genetic code diagram showing the amino acid residues as target of modification. Non-standard amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis. These modifications are often essential for the function or regulation of a protein.
For example, the carboxylation of glutamate allows for better binding of calcium cations, and the hydroxylation of proline is critical for maintaining connective tissues.
Another example is the formation of hypusine in the translation initiation factor EIF5A through modification of a lysine residue. Such modifications can also determine the localization of the protein. For instance, the addition of long hydrophobic groups can cause a protein to bind to a phospholipid membrane. It is important to compare the structures of alanine and beta alanine. In alanine, the side-chain is a methyl group; in beta alanine, the side-chain contains a methylene group connected to an amino group, and the alpha carbon lacks an amino group.
The two amino acids, therefore, have the same formulae but different structures. CspA, CspB, and CspG, major cold shock proteins of Escherichia coli , are induced at low temperature under conditions that completely block protein synthesis. Fan, H. Transcription—translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.
Fang, L. Farnham, P. Effects of NusA protein on transcription termination in the tryptophan operon of Escherichia coli. Cell 29, — Feng, Y. Escherichia coli poly A -binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E. Fisher, J. Four-dimensional imaging of E.
Folichon, M. Franch, T. Programmed cell death in bacteria: translational repression by mRNA end-pairing. French, S. Transcription and translation are coupled in Archaea. Frieda, K. Direct observation of cotranscriptional folding in an adenine riboswitch.
Gaal, T. Colocalization of distant chromosomal loci in space in E. Gebhardt, M. Widespread targeting of nascent transcripts by RsmA in Pseudomonas aeruginosa.
Giuliodori, A. Cell 37, 21— Golomb, M. Characterization of T7-specific ribonucleic acid polymerase. Resolution of the major in vitro transcripts by gel electrophoresis. PubMed Abstract Google Scholar. Goodson, J. LoaP is a broadly conserved antiterminator protein that regulates antibiotic gene clusters in Bacillus amyloliquefaciens. Processive antitermination. Govindarajan, S. Where are things inside a bacterial cell?
Gowrishankar, J. Why is transcription coupled to translation in bacteria? Graumann, P. A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures. Gray, W. Nucleoid size scaling and intracellular organization of translation across bacteria. Gultyaev, A. Guo, X. Structural basis for NusA stabilized transcriptional pausing. Cell 69, — Guo, Z.
Rotation of the head of the 30S ribosomal subunit during mRNA translocation. Solution structure of YaeO, a rho-specific inhibitor of transcription termination. Hadjeras, L. Detachment of the RNA degradosome from the inner membrane of Escherichia coli results in a global slowdown of mRNA degradation, proteolysis of RNase E and increased turnover of ribosome-free transcripts.
Hajnsdorf, E. Host factor Hfq of Escherichia coli stimulates elongation of poly a tails by poly A polymerase I. Hanna, M. Hao, Z. Pre-termination transcription complex: structure and function. Cell 81, 1— Hauryliuk, V. Recent functional insights into the role of p ppGpp in bacterial physiology. Heberling, T. A mechanistic model for cooperative behavior of co-transcribing RNA polymerases.
PLoS Comput. Heidrich, N. The small untranslated RNA SR1 from the Bacillus subtilis genome is involved in the regulation of arginine catabolism. Herskovits, A. Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle.
Hobot, J. Shape and fine structure of nucleoids observed on sections of ultrarapidly frozen and cryosubstituted bacteria. Hoffmann, S. Characterizing transcriptional interference between converging genes in bacteria. ACS Synth. Holmqvist, E. Acta — Gene Regul. Cell 70, — RNA-binding proteins in bacteria. Grad-seq shines light on unrecognized RNA and protein complexes in the model bacterium Escherichia coli.
Horn, G. Structure and function of bacterial cold shock proteins. Iost, I. The stability of Escherichia coli lacZ mRNA depends upon the simultaneity of its synthesis and translation.
Irastortza-Olaziregi, M. RNA localization in prokaryotes: where, when, how, and why. Wiley Interdiscip. RNA , e Irie, Y. Pseudomonas aeruginosa biofilm matrix polysaccharide Psl is regulated transcriptionally by RpoS and post-transcriptionally by RsmA. Irnov, I. A regulatory RNA required for antitermination of biofilm and capsular polysaccharide operons in Bacillales.
Iyer, S. Distinct mechanisms coordinate transcription and translation under carbon and nitrogen starvation in Escherichia coli. Jerome, L. Jiang, W. Jin, D. Role of RNA polymerase and transcription in the organization of the bacterial nucleoid. Johansson, J. RNA thermosensors in bacterial pathogens. Johnson, G. Functionally uncoupled transcription—translation in Bacillus subtilis.
Johnson, J. B12 cofactors directly stabilize an mRNA regulatory switch. Jonas, K. Complex regulatory network encompassing the Csr, c-di-GMP and motility systems of Salmonella typhimurium.
Joyeux, M. Colloid Interface Sci. A segregative phase separation scenario of the formation of the bacterial nucleoid. Soft Matter 14, — Kaberdin, V. Translation initiation and the fate of bacterial mRNAs. FEMS Microbiol. Kalapos, M. Identification of ribosomal protein S1 as a poly a binding protein in Escherichia coli.
Biochimie 79, — Kambara, T. Pervasive targeting of nascent transcripts by Hfq. Cell Rep. Kang, J. RNA polymerase accommodates a pause RNA hairpin by global conformational rearrangements that prolong pausing.
Structural basis for transcript elongation control by NusG family universal regulators. Kannaiah, S. Protein targeting via mRNA in bacteria. Acta, Mol. Cell Res. Spatiotemporal organization of the E. Cell 76, — Katsowich, N. Host cell attachment elicits posttranscriptional regulation in infecting enteropathogenic bacteria.
Kavita, K. Khong, A. The landscape of eukaryotic mRNPs. RNA 26, — Khosa, S. Kim, S. Kim, J. Spatial organization of the gene expression hardware in Pseudomonas putida.
Kohler, R. Architecture of a transcribing-translating expressome. Komarova, A. AU-rich sequences within 5' untranslated leaders enhance translation and stabilize mRNA in Escherichia coli. Protein S1 counteracts the inhibitory effect of the extended Shine-Dalgarno sequence on translation.
RNA 8, — Kortmann, J. Bacterial RNA thermometers: molecular zippers and switches. Kriner, M. Kristiansen, K. RNA 22, — Kurkela, J. Revealing secrets of the enigmatic omega subunit of bacterial RNA polymerase. Ladouceur, A. Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid-liquid phase separation. Larson, M. A pause sequence enriched at translation start sites drives transcription dynamics in vivo.
Lawson, M. Mechanism for the regulated control of bacterial transcription termination by a universal adaptor protein. Le Derout, J. Le, T. Molecular highways—navigating collisions of DNA motor proteins. Lewis, P. Compartmentalization of transcription and translation in Bacillus subtilis. Li, S. Escherichia coli translation strategies differ across carbon, nitrogen and phosphorus limitation conditions.
Li, R. Effects of cooperation between translating ribosome and RNA polymerase on termination efficiency of the rho-independent terminator. Libby, E. Membrane protein expression triggers chromosomal locus repositioning in bacteria. Lindahl, L. Transcription of the s10 ribosomal protein operon is regulated by an attenuator in the leader. Cell 33, — Lopez, M. Interactions of the major cold shock protein of Bacillus subtilis CspB with single-stranded DNA templates of different base composition.
Mahbub, M. Plants 6, — Makarova, O. Malabirade, A. Membrane association of the bacterial riboregulator Hfq and functional perspectives. Maquat, L. The pioneer round of translation: features and functions. Masachis, S. Type I toxin-antitoxin systems: regulating toxin expression via Shine-Dalgarno sequence sequestration and small RNA binding. Mascarenhas, J. Specific polar localization of ribosomes in Bacillus subtilis depends on active transcription. EMBO Rep. Mechold, U.
Differential regulation by ppGpp versus pppGpp in Escherichia coli. Melamed, S. Michaux, C. Miller, O. Visualization of bacterial genes in action. Milon, P. The nucleotide-binding site of bacterial translation initiation factor 2 IF2 as a metabolic sensor.
Mironov, A. Sensing small molecules by nascent RNA: a mechanism to control transcription in bacteria. Mitkevich, V. Moffitt, J. Spatial organization shapes the turnover of a bacterial transcriptome. Mogridge, J. Mohanty, B. The majority of Escherichia coli mRNAs undergo post-transcriptional modification in exponentially growing cells.
Mohapatra, S. Spatial distribution and ribosome-binding dynamics of EF-P in live Escherichia coli. MBio 8:e Functional mapping of the E. Moll, I. RNA 9, — Mondal, J. Entropy-based mechanism of ribosome-nucleoid segregation in E. Montero Llopis, P. Spatial organization of the flow of genetic information in bacteria. Nature , 77— Mooney, R. Regulator trafficking on bacterial transcription units in vivo. Cell 33, 97— Two structurally independent domains of E.
Morita, M. RNA Biol. Mustafi, M. Simultaneous binding of multiple EF-Tu copies to translating ribosomes in live Escherichia coli. MBio 9:e Muthunayake, N. Phase-separated bacterial ribonucleoprotein bodies organize mRNA decay.
RNA e Nevo-Dinur, K. Translation-independent localization of mRNA in E. In-cell architecture of an actively transcribing-translating expressome. Pal, K. Vibrio cholerae YaeO is a structural homologue of RNA chaperone Hfq that inhibits rho-dependent transcription termination by dissociating its hexameric state. Pannuri, A. Translational repression of NhaR, a novel pathway for multi-tier regulation of biofilm circuitry by CsrA.
Papenfort, K. Parry, B. The bacterial cytoplasm has glass-like properties and is fluidized by metabolic activity. Paul, B. Pei, X. Persson, F. Extracting intracellular diffusive states and transition rates from single-molecule tracking data.
Methods 10, — Phadtare, S. The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells. Nucleic acid melting by Escherichia coli CspE. Three amino acids in Escherichia coli CspE surface-exposed aromatic patch are critical for nucleic acid melting activity leading to transcription antitermination and cold acclimation of cells. Pichoff, S. An Escherichia coli gene yaeO suppresses temperature-sensitive mutations in essential genes by modulating rho-dependent transcription termination.
Plochowietz, A. Polissi, A. Changes in Escherichia coli transcriptome during acclimatization at low temperature. Potrykus, K.
Potts, A. Global role of the bacterial post-transcriptional regulator CsrA revealed by integrated transcriptomics. Pourciau, C. Regulation of iron storage by CsrA supports exponential growth of Escherichia coli.
MBio e Prilusky, J. Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs. Proshkin, S. Cooperation between translating ribosomes and RNA polymerase in transcription elongation. Qayyum, M. Transcription elongation factor NusA is a general antagonist of rho-dependent termination in Escherichia coli.
Rabhi, M. Ratje, A. Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites. Ray, S. Kinetics coming into focus: single-molecule microscopy of riboswitch dynamics. Da, Das, M. Interplay of cold shock protein E with an uncharacterized protein, YciF, lowers porin expression and enhances bile resistance in Salmonella Typhimurium. Rennella, E. RNA binding and chaperone activity of the E. Richards, J. Cell 74, — Richardson, J.
Preventing the synthesis of unused transcripts by rho factor. Cell 64, — Roberts, J. Mechanisms of bacterial transcription termination. Roggiani, M. Chromosome-membrane interactions in bacteria. Romeo, T. Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties. Rudner, D. Protein subcellular localization in bacteria.
Sahr, T. The Legionella pneumophila genome evolved to accommodate multiple regulatory mechanisms controlled by the CsrA-system. PLoS Genet.
Said, N. Science eabd Salvail, H. Sanamrad, A. Single-particle tracking reveals that free ribosomal subunits are not excluded from the Escherichia coli nucleoid.
Sanchez-Vazquez, P. Genome-wide effects on Escherichia coli transcription from ppGpp binding to its two sites on RNA polymerase. Santangelo, T. Termination and antitermination: RNA polymerase runs a stop sign. Saxena, S. Escherichia coli transcription factor NusG binds to 70S ribosomes. Schlax, P. Importance of an mRNA conformational switch and a ternary entrapment complex.
Schmidt, M. Schuwirth, B. Structures of the bacterial ribosome at 3. Sedlyarova, N. Natural RNA polymerase aptamers regulate transcription in E. Cell 67, 30— Sen, R. Nus factors of Escherichia coli. EcoSal Plus 6, 1— Sevostyanova, A. An RNA motif advances transcription by preventing rho-dependent termination.
Shaham, G. Genome scale analysis of Escherichia coli with a comprehensive prokaryotic sequence-based biophysical model of translation initiation and elongation. DNA Res. Sheng, H. Nucleoid and cytoplasmic localization of small RNAs in Escherichia coli.
0コメント