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NusA termination

The nusA gene protein of Escherichia coli and N gene protein of bacteriophage lambda interact in vitro and cooperate in vivo to prevent transcription termination. In vitro the nusA gene protein causes RNA polymerase to pause in the tR2 terminator region of lambda DNA A completed termination event at tR2 requires both the nusA gene protein and the previously described E. coli termination factor rho . In vitro the nusA gene protein causes RNA polymerase to pause in the tR2 terminator region of lambda DNA [2] As a termination factor, NusA mediates Rho-independent termination, depending on the DNA/RNA sequence 3. NusA can also modulate Rho activity to stimulate or inhibit Rho-dependent termination 4, 5,.. Although NusA is known to stimulate intrinsic termination in vitro, the in vivo targets and global impact of NusA are not known because it is essential for viability. Using genome-wide 3′.. We found that a functional NusA is necessary for efficient termination events to occur at both GTTE1 and 2. To enhance termination at GTTE1 in conditions in which the transcript is free of ribosomes, NusA acts at the same step as NusB and NusE/S10. In the presence of concomitant translation, termination at GTTE1 is dependent on the relative position of the translation stop codon and boxA. If translation stops upstream of boxA, NusA acts at the same step as NusB enhance termination. Ribosomes.

NusA and NusG are transcription factors that stimulate RNA polymerase pausing in Bacillus subtilis.While NusA was known to function as an intrinsic termination factor in B. subtilis, the role of NusG in this process was unknown.To examine the individual and combinatorial roles that NusA and NusG play in intrinsic termination, Term-seq was conducted in wild type, NusA depletion, ΔnusG, and. NusG is an intrinsic transcription termination factor that stimulates motility and coordinates gene expression with NusA. Zachary F Mandell, Reid T Oshiro, Alexander V Yakhnin, Rishi Vishwakarma, Mikhail Kashlev, Daniel B Kearns, Paul Babitzke. These include three host Nus proteins, NusA, B, and C. NusA is an interesting protein. By itself in E. coli, it is part of the transcription termination system. However, when co-opted by N, it participates in antitermination. The complex must act on RNA polymerase to ensure that the enzyme can no longer respond to the terminator. The variable locations of th

Termination of transcription by nusA gene protein of

NusA-AR1 interacts with N protein of phage λ, but is not essential for N-mediated suppression of transcription termination (antitermination) (15-17). NusA-AR2 can bind either to the CTD of the RNAP α-subunit (αCTD) or to the NusA-SKK. NusA-AR2 attached to NusA-SKK autoinhibits NusA activity by preventing RNA binding (15, 18) Intrinsic, or rho-independent termination, is a process in prokaryotes to signal the end of transcription and release the newly constructed RNA molecule. In prokaryotes such as E. coli, transcription is terminated either by a rho-dependent process or rho-independent process.In the Rho-dependent process, the rho-protein locates and binds the signal sequence in the mRNA and signals for cleavage Status. Unreviewed - Annotation score: Annotation score:2 out of 5. The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score cannot be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein NUSA has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by NUSA itself. We selected most functions NUSA had, and list some proteins which have the same functions with NUSA. You can find most of the proteins on our site Rho-unabhängige Termination (Intrinsische Termination) Bei dieser Form der Termination kommt es zur Ausbildung einer haarnadelförmigen Sekundärstruktur im RNA-Transkript. Der Grund für diese Haarnadelstruktur liegt in der speziellen Basenfolge. Daneben liegt oft ein U-reicher Bereich vor.Für die optimale Struktur eines intrinsischen Terminators werden damit folgende Regionen im Transkript.

Regulatory mechanism. stringent response: negative regulation, in stringent response. NusA: attenuation, NusA stimulates termination [Reference|http://www.nature.com/articles/nmicrobiol20157], in NusA regulon Transcription termination/antitermination protein NusA Add BLAST 347 <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p> Interaction

WikiGenes - nusA - transcription termination

Finally, NusA-stimulated termination is co-operative, suggesting that binding of multiple NusA molecules influences termination. Expression of the Bacillus subtilis tryptophan biosynthetic (trpEDCFBA) operon is negatively regulated in response to tryptophan by thetrp RNA-binding attenuation protein (TRAP) (reviewed in refs. 1 and 2). TRAP-mediated regulation of the trp operon includes. Model of NusA-dependent and NusG-dependent intrinsic termination of transcription of DNA into RNA. A new study shows that NusA and NusG together facilitate termination at about 88% of the.

Finally, NusA-stimulated termination is cooperative, suggesting that binding of multiple NusA molecules influences termination. * The trp RNA-binding attenuation protein (TRAP) regulates expression of the Bacillus subtilis trpEDCFBA operon by transcription attenuation and translation control mechanisms. Both mechanisms require the binding of tryptophan-activated TRAP to the 11 (G/U)AG-repeat. NusA and NusG are transcription elongation factors that stimulate RNA polymerase pausing in Bacillus subtilis . While NusA was known to function as an intrinsic termination factor, the role of NusG in this process had not been explored. To examine the individual and combinatorial roles that NusA and NusG play in intrinsic termination, Term-seq was conducted in wild type, NusA depletion, Δ. Its participation in Rho-dependent transcription termination has been perceived, but the molecular nature of this involvement is not known. We hypothesized that, because both Rho and NusA are RNA-binding proteins and have the potential to target the same RNA, the latter is likely to influence the global pattern of the Rho-dependent termination

Escherichia coli transcription termination factor NusA

  1. ation, and ter
  2. ation, supported by NusA and NusG, is required to suppress the toxic activity of foreign genes N-ter
  3. ation is strongly stimulated by NusA (Whalen et al. 1988). In vivo, a nusA deletion (in the background of a Rho-defective host) supports not only the growth of λ, but of a λN − mutant (Zheng & Friedman 1994). Suppression of lambda ter
  4. ation complex at the λnut RNA has evolved : After RNAP has synthesized λnut RNA, NusE and NusB bind to boxA, and NusA binds to spacer facilitated by NusA AR2 interaction with the C-ter
  5. ation wird durch zwei Mechanismen ausgeführt: Die intrinsische Ter

A new study, led by Penn State researchers, shows that NusG and the related protein, NusA, together facilitate termination at about 88% of the intrinsic terminators in the bacteria Bacillus subtilis R Transcription termination factor NusA, C-terminal duplication (IPR010214) Description. This superfamily represents an alpha-helical bundle domain, which has a SAM domain-like fold. This compact domain consists of a 4-5 helical bundle of two orthogonally packed alpha-hairpins, and contains one classic and one pseudo HhH (helix-hairpin-helix) motif. This domain is found at N-terminal of the. NusA is a key component in both Prevention and enhancement of transcriptional termination. It is important in both Rho-dependent and intrinsic termination, as well as in lambda and other phage antitermination systems. The gene was first identified by isolation of the nusAl mutation, which restricts bacteriophage l growth by preventing the antitermination activity of the l N protein. NusA is. Since NusA lacking the 79 C-terminal amino acids binds RNA alone and is proficient in transcription termination (23, 24), it is surprising that the nusA97 mutation, which results in the substitution of 23 amino acids encoded by the +1 reading frame for the C-terminal 84 amino acids of NusA (due to a deletion of 1 nt in codon 412), confers a reduced termination at the internal terminators of. NusA is an important player in both prevention and enhancement of transcriptional termination. NusA is important both in Rho-dependent and intrinsic termination, as well as in lambda and other phage antitermination systems. The NusA gene was first identified by isolation of the nusAl mutation, which limits bacteriophage-l growth by preventing the antitermination activity of the l N protein.

NusA-dependent transcription termination prevents

Compromised Factor-Dependent Transcription Termination inSDS-PAGE profile of the archaeal NusA protein

NusA modulates intragenic termination by different pathway

NusG is an intrinsic transcription termination factor that

Finally, NusA-stimulated termination is cooperative, suggesting that binding of multiple NusA molecules influences termination. The trp RNA-binding attenuation protein (TRAP) regulates expression of the Bacillus subtilis trpEDCFBA operon by transcription attenuation and translation control mechanisms. Both mechanisms require the binding of tryptophan-activated TRAP to the 11 (G/U)AG-repeat. DOI: 10.1074/jbc.M115.701268 Corpus ID: 19629355. Transcription Elongation Factor NusA Is a General Antagonist of Rho-dependent Termination in Escherichia coli* @article{Qayyum2016TranscriptionEF, title={Transcription Elongation Factor NusA Is a General Antagonist of Rho-dependent Termination in Escherichia coli*}, author={M. Qayyum and Debashish Dey and R. Sen}, journal={The Journal of. The nusA protein serves as an antitermination factor, RNA polymerase subunit, and true termination factor at some terminator sites. In general, termination at T1 in vitro is quiteefficient with an 80% effectiveness rate without any additional factors. In vivo and in E. coliextracts, the T1 terminator has shown to be nearly 100% efficient. In an isolated and purified system with only nusA. A total of 88% of all intrinsic termination sites relied on NusA or NusG in some capacity. Intrinsic termination is clearly not completely 'factor-independent.' The researchers are still investigating the precise role that the Nus proteins play in transcription termination. We think that NusA helps directly in the formation of the hairpins required for intrinsic termination and that.

The essential bacterial transcription factor NusA stimulates both pausing and termination of transcription, thus playing a central role. Here, we report single-particle electron cryo-microscopy reconstructions of NusA bound to paused E. coli RNAP elongation complexes with and without a pause-enhancing hairpin in the RNA exit channel. The structures reveal four interactions between NusA and.

In M. pneumoniae, the bacterial elongation and termination factor NusA couples RNAP and the ribosome (O'Reilly et al., 2020). Commonly, bacterial NusA proteins contain an N-terminal domain (binds RNAP), and a S1 and two KH domains (bind RNA) S. 378 - Termination Justification Act Amendment of 2021 S. Con. Res 17 - Unbar of Brentvx S. 384 - Freedom of Choice H.R. 335- To merge the Bureau of Prisons into the United States Marshal Services. H.R. 389 - WH Transparency Act H.R. 390 - Law Enforcement Reform Act of 2021 H. Res. 15 - To expel KooIthing from the House of Representatives H.R. 391 - Establishment of the Department of. NusA protein also enhances termination at trp t, an effect similar to the low UTP response. Further, termination can be slightly improved by including rho factor, resulting in an overall efficiency of almost 100% at trp t NusA functions are not recovered even when transcription with mutant RNAP is done with excess NusA, a condition which does restore NusA‐RNA crosslinking. By affinity chromatography, we show that NusA interacts directly with alpha, and also with beta and beta', but not with mutant alpha. Hence, alpha‐NusA interaction is vital for the control of transcript elongation and termination

The Nus factors—NusA, NusB, NusE, and NusG—area set of well-conserved proteins in bacteria and are involved in transcription elongation, termination, antitermination, and translation processes. Originally, Escherichia coli host mutations defective for supporting bacteriophage λ N-mediated antitermination were mapped to the nusA (nusA1), nusB (nusB5, nusB101), and nusE (nusE71) genes, and. IMAGE: Model of NusA-dependent and NusG-dependent intrinsic termination of transcription of DNA into RNA.A new study shows that NusA and NusG together facilitate termination at about 88% of the. Bei der Rho-Faktor-abhängigen Termination sind keine destabilisierenden Sequenzelemente in der RNA nötig, denn die Termination wird durch den Terminationsfaktor Rho katalysiert, einen hexameren Proteinkomplex. Die Destabilisierung des transkriptionalen Komplexes ist Folge der Helikaseaktivität des Rho-Faktors. Rho erkennt hierbei C-reiche (und G-arme) Abschnitte auf dem Transkript NusA-dependent terminators tend to have weak RNA hairpins and/or distal U-tract interruptions. Our unpublished studies indicate that NusG is another intrinsic termination factor. We are exploring the interrelationship between NusG-dependent pausing and NusG-dependent termination. Our hypothesis is that NusG stimulates pausing prior to. Additionally, the elongation protein factor NusA interacts with the RNA polymerase and the hairpin structure to stimulate transcriptional termination. بالإضافة، يتأثر بروتين عامل الاستطالة NusA مع بوليميراز الرنا وبنية الحلقة الجذعية لاستثارة إنهاء النسخ

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists However, NusA is not an affinity tag. Thus, it is typically coupled to the his 6-tag to facilitate purification (de Marco, 2006). Finally, it is also large (55 kDa), which can sometimes make proteolytic removal of the NusA fusion protein difficult. Recently developed tags: SET. It was also recently shown that small highly acidic peptide tags.

Antitermination - Wikipedi

Termination can be controlled with the same sort of precision as initiation. NusA, B, and C. NusA is an interesting protein. By itself in E. coli, it is part of the transcription termination system. However, when co-opted by N, it participates in antitermination. The complex must act on RNA polymerase to ensure that the enzyme can no longer respond to the terminator. The variable locations. NusA and the other antitermination factors NusB, NusE (ribosomal protein S10) and NusG combine with these consensus sequences and interact with RNA polymerase, rendering it insensitive to termination by rho-dependent terminators that occur throughout the long (5.5 kb) pre-rRNA transcript. It has been proposed that an antitermination mechanism exists in bacterial rrns to overcome the. A total of 88% of all intrinsic termination sites relied on NusA or NusG in some capacity. Intrinsic termination is clearly not completely 'factor-independent.' The researchers are still investigating the precise role that the Nus proteins play in transcription termination. We think that NusA helps directly in the formation of the hairpins required for intrinsic termination and that NusG is.

[nUSA] United States Marshal Service | 2020 Tampering of any card is prohibited and will result in a termination and a blacklist. If you have any questions regarding this board DM the Chief of Staff+ Label Library Board Access Lis We have mapped three Escherichia coli RNA polymerase mutations selected by Guarente (1979) to suppress the termination defects of rho201. We find that two of the mutations are located in the 3′ half of the rpoB gene encoding the β subunit. The third mutation is in the rpoC gene, encoding the β′ subunit. All three RNA polymerase mutations affect termination efficiency, even in rho. When NusA is present, RNA crosslinks to NusA rather than to α. We show that this NusA-RNA interaction is diminished during transcription with an RNAP mutant that lacks the C-terminus of α beyond amino acid 235, including the so-called αCTD. The absence of αCTD also affects NusA's ability to enhance transcription pausing, termination at.

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NusA directly interacts with antitermination factor Q from phage λ [22.04.20] Q-dependent anti-termination (AT) is the second mechanism lambdoid phages use to suppress termination signals. N-mediated AT is the best studied AT mechanism by now, whereas only little is known about AT relying on factor Q. This study unravels and characterizes the. Roles of NusA and 1,4 in termination sequence effects on termination and pausing have also been reported in other systems (Telesnitsky and Cham- berlin 1989; Lee et al. 1990; Reynolds and Chamberlin 1992). For quantitation of the amount of attenuated transcripts, we pooled the two RNA classes. L4 stabilizes a NusA-dependent pause at the attenuation site Our previous experiments showed that. The proteins NusA and NusG, which are essential for viability of wild-type Escherichia coli, participate in various post-initiation steps of transcription including elongation, antitermination, and termination. NusG is required along with the essential Rho protein for factor-dependent transcription termination (also referred to as polarity), but the role of NusA is less clear with conflicting.

The transcription termination factor NusA from Aeropyrum pernix was crystallized using a counter‐diffusion technique in both terrestrial and microgravity environments. Crystallization under microgravity conditions significantly reduced the twinning content (1.0%) compared with terrestrially grown crystals (18.3%) and improved the maximum resolution from 3.0 to 2.29 Å, with similar unit. premature termination of transcription. Thus, NusA-dependent coupling should be less important in a mutant with low Rho activity. The fact that E. coli grows without NusA argues that NusA should be considered an accessory factor rather than a subunit of RNA polymerase. Transcription elongation can be considered to include all events in transcription that follow initiation and precede. Transcription termination in prokaryotes can be rho-independent (intrinsic terminators exist in the RNA polymerase) and rho-dependent, i.e., the RNA polymerase requires the cofactor rho for termination of transcription. The terminator regions in various systems have similar structures. They consist of palindromic sequences that can fold back into a hairpin. In the rho-independent terminator. Instead, NusA-stimulated termination in its 5'UTR dictates the extent of transcription into the operon. Another major focus of this thesis is to understand the regulation of transcription elongation by NusG-stimulated pausing of RNA polymerase. NusG is a positive elongation factor in E. coli that accelerates transcription by reducing the dwell time of RNA polymerase at pause sites. In B.

Rcgions of NusA important for enhancement of termination irl vitro 64 N binds a carboxy-terminal region of NusA 66 Region3 of' NusA necessary for enhancement of antitermination by N 68 The effects of NusA deletions of the formation of N-NusA-riicr site complexes 71 The effects of NusA deletions on the formation of cornpletc complexes contüining N. the NusA factors and RNA polymerase 73. The transcription termination anti-termination factor, also known as N-utilization substance A (NusA), is a 55 kDa hydrophilic protein that promotes the soluble expression of even very hydrophobic fusion proteins in E. coli . In E. coli, wild-type NusA promotes pauses in DNA transcription by RNA polymerase . Because transcription and. PPP-, Multi-Link-PPP- and HDLC-termination: VoIP media gateways: SIP: Interfaces - Uplink, Cascading, Management 1 or 10 Gigabit Ethernet: 2 x optical SFP+ based and 3 x electrical: SDH: 2 x STM-16/4, 2 x STM-4/1, 4 x 100/1000BaseT per SDH-unit: Management: 10/100BaseT for local configuration 10/100/1000BaseT for central management: Interfaces - User Side Ports per Card; Ethernet (optical.

Crystal structure of archaeal transcription termination factor NusA: 2cy1: Crystal structure of APE1850: 2dgr: Solution structure of the second KH domain in ring finger and KH domain containing protein 1: 2e3u: Crystal structure analysis of Dim2p from Pyrococcus horikoshii OT3: 2e5l: A snapshot of the 30S ribosomal subunit capturing mRNA via the Shine- Dalgarno interaction : 2f4v: 30S ribosome. The factor nusA is involved in the function of elongation as well as chain termination. The antibiotic rifampicin can bind with the beta subunit of the bacterial RNA polymerase. Thereby, it is preventing the enzyme from initiating bacterial RNA polymerization. Another antibiotic known as streptolydigin inhibits the elongation process of bacterial RNA polymerization. The prokaryotes mRNA is. Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 Å resolution Journal of Molecular Biology, 2001 Eleanor Dodso The NusA protein binds to the elongating RNA polymerase, competitively with the σ subunit. Once the transcription is complete, NusA dissociates from the enzyme, the RNA polymerase dissociates from the DNA and σ factor can now bind to the enzyme to initiate transcription. 27. Termination of RNA synthesis 1. Intrinsic Termination - RNA transcript with self-complementary sequences Permitting. nusA Transcription termination protein NusA Campylobacter jejuni subsp. jejuni S3 (complete) Arnit_2828 transcription termination factor NusA Arcobacter nitrofigilis DSM 7299 (complete) CCC13826_0599 nusA

Structural basis for transcription antitermination at

NusA with RNA polymerase increases pausing and the efÆciency of termination at intrinsic terminators. NusA is also part of the phage l N protein-modiÆed antitermination complex that functions to prevent transcriptional termination. We have investigated the structure of NusA using various deletion fragments of NusA in a variety of in vitro assays. Sequence and structural alignments have. Rho-dependent termination requires Rho factor but not NusA. B. Rho-independent termination requires NusA but not Rho. Antibiotics That Affect Transcription. Antibiotics must meet two fundamental criteria: They must kill or retard the growth of a pathogen, and they must not harm the host. Rifamycin B . Selectively binds to the bacterial RNA pol. Inhibits transcription initiation. Actinomycin D. Effects of NusA protein on transcription termination in the tryptophan operon of Escherichia coli. Cell 29:945-951. Crossref. PubMed. Google Scholar. 88. Schmidt MC, Chamberlin MJ. 1987. nusA protein of Escherichia coli is an efficient transcription termination factor for certain terminator sites. J Mol Biol 195:809-818. Crossref. PubMed. Google Scholar. 89. Toulokhonov I, Artsimovitch I. Gene nusA from Persephonella marina EX-H1: transcription termination factor NusA Jump to section on this page: Summary Actions Predictions Experimental Validation Supporting Info Pathway Information Linked Genes phenotype. Hide | Top. Summary. Member of NCBI Protein Clusters CLSK2479484(See COMBREX Page) (See NCBI page) NCBI Entrez GeneID 7676051: UniProtKB accession C0QTL7; RefSeq Protein. Transcription in Prokaryotes (bacteria) animated: The process of synthesis of RNA by copying the template strand of DNA is called transcription. During repli..

Both types of termination involve NusA protein. D. None of the above are correc. A. Both types of termination occur following a pause by the polymerase. 49. The process by which the base sequence of all or a portion of a DNA molecule is used to direct the synthesis of an RNA molecule is called A. replication. B. transcription. C. reverse transcription. D. translation. B. transcription. 50. Key. Transcription termination factor NusA Lactobacillus fermentum CECT 5716 (complete) LSL_0569 nusA transcription elongation factor NusA Lactobacillus salivarius UCC118 (complete) HN6_00509 nusA N utilization substance protein A Lactobacillus salivarius CECT 5713 (complete). Termination der Translation: Stoppkodon (UAA in E. coli) Translation. E. coli. stopcodon. Kozak-Sequenz bei Eukaryoten. 10. Multiple Klonierungsstelle. multiple cloning site (MCS) im Anschluss an die Kontrollregionen des Expressionsvektors Sequenz mit verschiedenen Schnittstellen für Restriktionsendonukleasen zum Einbringen einer Gensequenz in den Expressionsvektor Schnittstellen sind. PT. Bawana Margatama. 252 likes. PT Bawana Margatama is one of the largest Manpower Management Company who has growth in manpower over 2000 employees this year. Currently we are seeking good..

(PDF) Termination and antitermination: RNA polymerase runsCircular dichroism (CD) shows the secondary structure

The head of the regional disaster management agency (BPBD) in East Nusa Tenggara (NTT) was removed from his position this week, after the governor said he had been unresponsive amid deadly flash floods and landslides that killed at least 138 people and drove thousands out of their homes on Sunday. The firing was confirmed by NTT regional secretary Benediktus Polo Maing, who said that NTT. The infB gene is part of the polycistronic nusA operon containing metY (minor form of the initiator tRNA), ylxC (protein of unknown function), nusA (a transcriptional termination factor), infB (translation initiation factor IF2), rbfA (ribosome binding factor A), truB (tRNA pseudouridine 5S synthase), rpsO (ribosomal protein S15), and pnp (polynucleotide phosphorylase) Swiss-Belhotel Segara in Nusa Dua Declared Bankrupt. Tribun-Bali.com reports that the Supreme Court of Indonesia declared the Swiss-Belhotel Segara at Nusa Dua in Bali had been formally declared bankrupt on 14 September 2020.. Hendrik Rumapea, general manager of The Swiss-Belhotel Segara, voiced his displeasure with the Court's decision on Thursday, 28 January 2021, said: I object if the. Termination and antitermination complexes that are being studied in the von Hippel laboratory. vonhippelfig.gif; Publications. Greive S.J. and P.H. von Hippel. (2005) Thinking quantitatively about transcriptional regulation. Nat Rev Mol Cell Biol 6:221-32. Johnson N.P., W.A. Baase, and P.H. Von Hippel (2004) Low-energy circular dichroism of 2-aminopurine dinucleotide as a probe of local.

nusA - Probable transcription termination protein NusA

Wijaya Engindo Nusa, Tanah Merah. 2,993 likes · 7 talking about this · 1 was here. MEMORIES IN TANGGU Gene nusA from Mycoplasma pneumoniae M129: transcription elongation factor NusA Jump to section on this page: Summary Actions Predictions Experimental Validation Supporting Info Pathway Information Linked Genes phenotype. Hide | Top. Summary . Member of NCBI Protein Clusters. Search the world's information, including webpages, images, videos and more. Google has many special features to help you find exactly what you're looking for

Transcriptional Polarity in rRNA Operons of EscherichiaHomestay Pasir Murah Gudang | MyCribBookingTranscriptional Pausing in the Bacillus subtilis pyr
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