ライフサイエンスコーパス: RNAP

1 RNAP clusters are sensitive to hexanediol, a chemical th

2 RNAP contains a clamp domain that closes around the nucl

3 RNAP is recycled when, after releasing trapped nucleic a

4 Structurally, phi14:2 RNAP is most similar to eukaryotic RNAPs that are involv

5 erference(6,7), although most of the phi14:2 RNAP structure (nearly 1,600 residues) maps to a new reg

6 These structures reveal how sigma(28) -RNAP recognizes promoter DNA through strong interactions

7 o better understand how living systems adapt RNAP resources, via the complementary pairing of constit

8 ption elongation factors dramatically affect RNAP pausing in vitro, but the genome-wide role of such

9 alternative transcription cycle that allows RNAP to reinitiate without dissociating from DNA, which

10 surprisingly is ~100-fold more potent as an RNAP inhibitor.

11 a coli RNAP, with or without TraR, and of an RNAP-promoter complex.

12 rate the value of this framework, we analyze RNAP number distribution data for ribosomal genes in Sac

13 d by RNase digestion (RNET-seq), we analyzed RNAP pausing in Bacillus subtilis genome-wide and identi

14 cation through the evolution of an ancestral RNAP two-barrel catalytic core.

15 transcription, in which a promoter-anchored RNAP uses a "scrunching" mechanism, has not.

16 he corresponding transcription activity, and RNAP redistributed into dispersed, smaller clusters when

17 tures of the RNAP, RNAP-TFEalpha binary, and RNAP-TFEalpha-promoter DNA ternary complexes from archae

18 Our structure supports a DNA-distortion and RNAP-non-contact paradigm of transcriptional activation

19 DSB repair and cSDR differ; certain DksA and RNAP mutants are able to support the first process, but

20 uman initiation complexes in the RNAP II and RNAP III systems at the single-molecule level under pico

21 for cells after transcription inhibition and RNAP degradation, we argue that translocating condensins

22 ddition and inducing dissociation of RNA and RNAP from DNA.

23 on by the housekeeping sigma(70) -associated RNAP.

24 SspA assembles with the sigma(70)-associated RNAP holoenzyme (RNAPsigma(70)), forming a virulence-spe

25 -electron microscopy structures of bacterial RNAP-promoter DNA complexes, including structures of par

26 ge proteins that interact with the bacterial RNAP and compare how two prototypical phages of Escheric

27 her lasso peptides that target the bacterial RNAP and provides a structural foundation to guide lasso

28 small proteins to "puppeteer" the bacterial RNAP to ensure a successful infection.

29 D prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elong

30 aining different-length mRNA spacers between RNAP and the ribosome active-center P site.

31 Antagonistic dynamics can also occur between RNAPs from divergently transcribed gene pairs.

32 global transcription regulator in MTB, binds RNAP and activates transcription by stabilizing the tran

33 inhibit transcription elongation by blocking RNAP with a protein bound to the DNA template.

34 Unexpectedly, the DNA-bound RNAP often restarts transcription, usually in reverse di

35 e can be melted and transcribed by the bound RNAPs as the enlarged DNA bubble can help the separation

36 ion factors NusG (which is thought to bridge RNAP and the ribosome) and NusA.

37 has been studied extensively, but pausing by RNAP during initial transcription, in which a promoter-a

38 GreA modulated translesion transcription by RNAP, depending on changes in the trigger loop structure

39 During transcription by RNAP, we directly observed rotational steps that corresp

40 repair(9), as well as from transcription by RNAP.

41 all molecule inhibitors which block the CarD/RNAP interaction and to understand the mechanisms by whi

42 NAP phylogeny revealed that the Caudovirales RNAP forms a clade distinct from cellular homologs, sugg

43 ecomes a barrier to RNAP elongation, causing RNAP stalling, backtracking, and transcriptional arrest.

44 fficiently and stably halts Escherichia coli RNAP transcription.

45 en intermediates containing Escherichia coli RNAP with the transcription factor TraR en route to form

46 ranslesion RNA synthesis by Escherichia coli RNAP without altering the fidelity of nucleotide incorpo

47 to determine structures of Escherichia coli RNAP, with or without TraR, and of an RNAP-promoter comp

48 or halting transcription by Escherichia coli RNAP.

49 meric Rho loads onto RNA prior to contacting RNAP and then translocates along the transcript in pursu

50 scription initiation in the stalk-containing RNAPs, including archaeal and eukaryotic RNAPs.

51 ic termination, an activity only of the core RNAP enzyme and transcript sequences that encode an RNA

52 Our results show that coupled RNAP-ribosome movement is not a general hallmark of bact

53 We suggest that cyanobacterial RNAP has a specific Trigger Loop domain conformation, an

54 Features of the cyanobacterial RNAP hydrolysis are reminiscent of the Gre-assisted reac

55 Using cyanobacterial RNAP as a model, we investigated alternative mechanisms

56 tures and supporting biochemical data define RNAP and promoter DNA conformational changes that deline

57 we show that this protein is a DNA-dependent RNAP that is translocated into the host cell along with

58 abundance during slow growth and a dimeric (RNAP-delta-HelD)(2) structure that resembles hibernating

59 We show that in relation to Eco RNAP, Mtb displays slower initial nucleotide incorporati

60 abilities relative to Escherichia coli (Eco) RNAP.

61 he interface between a NusG-bound elongating RNAP and the ribosome and propose that it can mediate tr

62 ucture that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzy

63 ing RNAPs, including archaeal and eukaryotic RNAPs.

64 , phi14:2 RNAP is most similar to eukaryotic RNAPs that are involved in RNA interference(6,7), althou

65 Here, we examined RNAP III lacking C37/53/C11 and various reconstituted fo

66 RNA exiting RNAP interacts with NusA before entering the central cha

67 ing a high fidelity of transcription and for RNAP arrest prevention.

68 ducing the availability of these factors for RNAP II transcription and contributing, at least in part

69 und in the active center, which is loose for RNAP III relative to other RNAPs.

70 ery can recruit protein factors required for RNAP II transcription.

71 the active site RNA 3' cleavage factors for RNAPs II and I.

72 nables display of nascent RNA molecules from RNAP in a minimal in vitro transcription reaction.

73 Strikingly, GreB-RNAP complexes never initiated at an rRNA promoter; only

74 rases (RNAPs) from bacteria to mammals halts RNAP in an elemental paused state from which longer-live

75 lity and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains el

76 the C-terminal domain of RNA polymerase II (RNAP II) and in the recruitment of the cleavage/polyaden

77 hat ATXN3 associates with RNA polymerase II (RNAP II) and the classical nonhomologous end-joining (C-

78 ve analysis revealed TraR-induced changes in RNAP conformational heterogeneity.

79 and a second fluorescent probe elsewhere in RNAP or in DNA, we detect and characterize TL closing an

80 unit and NTPase HelD have been implicated in RNAP recycling.

81 ion, we provide a mechanistic drug target in RNAP.

82 luorescence microscopy to observe individual RNAP molecules after transcript release at a terminator.

83 TraR binding induced RNAP conformational changes not seen in previous crystal

84 GreB did not alter initial RNAP-promoter binding but instead blocked a step after c

85 conformational rearrangement of the initial RNAP-promoter complex.

86 The liberated RNAP can either stay dormant, sequestered by HelD, or up

87 bited by GreB/DksA because their short-lived RNAP complexes do not allow sufficient time for SCFs to

88 the elongation efficiency of already-loaded RNAPs, causing premature termination and quick synthesis

89 delivery to the active site, thereby locking RNAP in an inactive state.

90 long the transcript in pursuit of the moving RNAP to pull RNA from it.

91 assay which monitors the association of MTB RNAP, native rRNA promoter DNA and CarD has been develop

92 ranscription and promoter escape for the Mtb RNAP.

93 strating that Sor inhibits the wild-type Mtb RNAP by a similar mechanism as Rif: by preventing the tr

94 Within these multimeric RNAP-encoding Caudovirales (mReC), we find that the simi

95 g that Sor inhibits the wild-type and mutant RNAPs through different mechanisms prompts future consid

96 We observed that although the mutant RNAPs stimulate translesion synthesis, their expression

97 Compared with the natural RNAP substrates, NTPs, the K(m) of RNAP for NDPs was inc

98 e accounted for by molecular modeling of NTP/RNAP co-crystal structures.

99 and in vivo, suggesting that it may nucleate RNAP clusters.

100 l organization and transcription activity of RNAP in E. coli cells using quantitative superresolution

101 r YjbH and ClpXP, complexes with alphaCTD of RNAP prior to binding the cspA promoter to repress cspA

102 cromolecular crowding affects association of RNAP to DNA, not much is known about how crowding acts o

103 fectively enhances the torsional capacity of RNAP.

104 Our study characterizes a clade of RNAP-encoding Caudovirales and suggests the ancient orig

105 RNAP and transiently widen the main cleft of RNAP to facilitate DNA promoter entering and formation o

106 ngly affect the nucleotide addition cycle of RNAP by increasing the rate of nucleotide addition but a

107 in the transcribed genes, and degradation of RNAP II relative to controls.

108 In contrast, the cellular distribution of RNAP closely followed the morphology of the underlying n

109 inal tails, and binds to the beta1 domain of RNAP.

110 nd switch 2-universal structural features of RNAP-in restricting access of DNA to the RNAP active sit

111 Surprisingly, a large fraction of RNAP clusters persisted in the absence of high rRNA tran

112 This negative effect appears independent of RNAP convoy formation and is abrogated by topoisomerase

113 The factors included two kinases of RNAP II (Bur1 and Ctk1), a histone demethylase (Jhd2), a

114 eover, we show that the expression levels of RNAP II-transcribed genes downstream of tRNA loci correl

115 e natural RNAP substrates, NTPs, the K(m) of RNAP for NDPs was increased ~4-fold, whereas the V (max)

116 Genomic mapping of RNAP and transcriptome profiles corresponding to the dif

117 rs providing insights into the mechanisms of RNAP and the evolution of the transcription machinery.

118 t five distinct mechanisms: (i) occlusion of RNAP binding; (ii) roadblocking RNAP progression; (iii)

119 Bdp1 for the high transcriptional output of RNAP III.

120 itor that binds in the Rif-binding pocket of RNAP.

121 We found rapid redistribution of RNAP across the genome, primarily at sigma70 promoters.

122 es that direct genome-wide redistribution of RNAP during the stress.

123 ription complex, the subsequent retention of RNAP on DNA constitutes a previously unidentified stage,

124 onformational dynamics of the active site of RNAP, with potential effects on cellular stress response

125 onformational changes in all the subunits of RNAP and transiently widen the main cleft of RNAP to fac

126 of the real-time positional trajectories of RNAP after a stall revealed the kinetic parameters of ba

127 A thorough understanding of RNAP and transcription factor function, and of the seque

128 measurements of cell-to-cell variability of RNAP numbers and interpolymerase distances can reveal th

129 which the beta' zinc-binding domain (ZBD) of RNAP stretches out from its canonical position to intera

130 The Cap binding determinant on RNAP overlaps, but is not identical to, that of MccJ25.

131 secondary events from the initial effects on RNAP.

132 dure enriched for direct effects of ppGpp on RNAP rather than for indirect effects on transcription r

133 he ECF sigma factor occupy the same sites on RNAP as in primary sigma factors, show that the connecto

134 ains with/without the ppGpp binding sites on RNAP.

135 es never initiated at an rRNA promoter; only RNAP molecules arriving at the promoter without bound Gr

136 Q loads onto RNAP engaged in promoter-proximal pausing at a Q binding

137 hich is loose for RNAP III relative to other RNAPs.

138 Our RNAP phylogeny revealed that the Caudovirales RNAP forms

139 consequence lifetime, of an elemental paused RNAP is modulated by backtracking, nascent RNA structure

140 mponents on bacteriophage T7 RNA polymerase (RNAP) activity using a common quantitative PCR instrumen

141 2alphabetabeta'omegaepsilon) RNA Polymerase (RNAP) core enzyme, sigma(A), a promoter DNA, and the lig

142 esis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from sta

143 transcript release precedes RNA polymerase (RNAP) dissociation from the DNA template much more often

144 Pausing by RNA polymerase (RNAP) during transcription elongation, in which a transl

145 Pausing by RNA polymerase (RNAP) during transcription regulates gene expression in

146 ion as a changing pattern of RNA polymerase (RNAP) flux along the DNA.

147 ription by the Mycobacterial RNA polymerase (RNAP) has previously been shown to exhibit different ope

148 RNA polymerase (RNAP) III synthesizes tRNAs and other transcripts, and m

149 nitiation factor Bdp1 in the RNA polymerase (RNAP) III system, however, remained elusive.

150 d RNAs) and transcription by RNA polymerase (RNAP) in all domains of life.

151 m for organizing clusters of RNA polymerase (RNAP) in Escherichia coli Using fluorescence imaging, we

152 ppGpp binds to two sites on RNA polymerase (RNAP) in Escherichia coli, but it has also been reported

153 NA binding cleft of cellular RNA polymerase (RNAP) is necessary for transcription initiation but the

154 cent studies have shown that RNA polymerase (RNAP) is organized into distinct clusters in Escherichia

155 -35 and -10 sites can buffer RNA polymerase (RNAP) kinetics against mutations and how promoters that

156 single-cell measurements of RNA polymerase (RNAP) molecules engaged in the process of transcribing a

157 anscription is punctuated by RNA polymerase (RNAP) pausing.

158 ation by binding directly to RNA polymerase (RNAP) rather than to promoter DNA.

159 r playing essential roles in RNA polymerase (RNAP) recycling, gene regulation, and genomic stability

160 During transcription, RNA polymerase (RNAP) supercoils DNA as it translocates.

161 tor associates with the core RNA polymerase (RNAP) to control most transcription initiation, while al

162 ic sigma factor that targets RNA polymerase (RNAP) to control the expression of flagella-related gene

163 ption is promoter melting by RNA polymerase (RNAP) to form the open promoter complex(1-3).

164 whether and how it modifies RNA polymerase (RNAP) to initiate transcription remains unclear.

165 ription system with purified RNA polymerase (RNAP) to investigate rRNA synthesis in the photoheterotr

166 The RNA polymerase (RNAP) trigger loop (TL) is a mobile structural element o

167 s of infection and that ASFV RNA polymerase (RNAP) undergoes promoter-proximal transcript slippage at

168 To generate RPo, RNA polymerase (RNAP) unwinds the DNA duplex to form the transcription b

169 DNA-directed RNA polymerase (RNAP) uses one strand of the DNA duplex as template to p

170 licated by the RNA-dependent RNA polymerase (RNAP) via a complementary RNA (cRNA) intermediate.

171 kinetically coordinate with RNA polymerase (RNAP)(3-11), forming a signal-integration hub for co-tra

172 essing enzymes that includes RNA polymerase (RNAP)(6), gyrase(2), a viral DNA packaging motor(7) and

173 a' subunits of multi-subunit RNA polymerase (RNAP), a high-resolution phylogenetic marker which enabl

174 p in the RNA exit channel of RNA polymerase (RNAP), inactivating nucleotide addition and inducing dis

175 e gatekeeper for the genome, RNA polymerase (RNAP), is among the most regulated enzymes.

176 transcription machinery, the RNA polymerase (RNAP), is often regulated by a variety of mechanisms inv

177 n and block RNA synthesis by RNA polymerase (RNAP), leading to subsequent recruitment of DNA repair f

178 g Mycobacterium tuberculosis RNA polymerase (RNAP), M. tuberculosis ECF sigma factor sigma(L), and pr

179 secondary channel of E. coli RNA polymerase (RNAP), such as GreA, GreB or DksA.

180 The expressome comprises RNA polymerase (RNAP), the ribosome, and the transcription elongation fa

181 RNA polymerase (RNAP), the transcription machinery, shows dynamic bindin

182 berculosis (Mtb) encodes the RNA polymerase (RNAP)-binding protein CarD, which is absent in E. coli b

183 epair mechanism that removes RNA polymerase (RNAP)-stalling DNA damage from the transcribed strand (T

184 ses in which the movement of RNA polymerase (RNAP)-synthesizing messenger RNA (mRNA) is coordinated w

185 the free-state of endogenous RNA polymerase (RNAP).

186 Rif targets the enzyme RNA polymerase (RNAP).

187 be utilized as substrates by RNA polymerase (RNAP).

188 ymatic target, the bacterial RNA polymerase (RNAP).

189 irect contact of TthCsm with RNA polymerase (RNAP).

190 ysis by the active centre of RNA polymerase (RNAP).

191 le to the speed of bacterial RNA polymerase (RNAP)].

192 en condensin and elongating RNA polymerases (RNAPs) and find that RNAPs are likely steric barriers th

193 ten transcribed by multiple RNA polymerases (RNAPs) at densities that can vary widely across genes an

194 Cellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening gen

195 RNA polymerases (RNAPs) contain a conserved 'secondary channel' which bin

196 pause sequence that acts on RNA polymerases (RNAPs) from bacteria to mammals halts RNAP in an element

197 Site-specific arrest of RNA polymerases (RNAPs) is fundamental to several technologies that asses

198 RNA polymerases (RNAPs) transcribe genes through a cycle of recruitment t

199 te in cellular multisubunit RNA polymerases (RNAPs)(5).

200 erase families but found in RNA polymerases (RNAPs).

201 Finally, the cellular power (RNAP and ribosome usage) required to maintain a circuit

202 ing previously undetected transient promoter-RNAP interactions that contribute to populating the inte

203 including the most prevalent clinical Rif(R) RNAP substitution found in Mtb infected patients (S456>L

204 Sor inhibits a subset of Rif(R) RNAPs, including the most prevalent clinical Rif(R) RNAP

205 stent with the notion that pre-tRNAs recruit RNAP II-associated factors, thereby reducing the availab

206 y which a helicase-like factor HelD recycles RNAP.

207 product at intrinsic termination, recycling RNAP diffuses on the DNA template for reinitiation most

208 role for transcription factors in regulating RNAP functionality and elongation.

209 fine HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.

210 proposed to promote termination by releasing RNAP-nucleic acid contacts.

211 GreB, a transcription factor known to rescue RNAP from the backtracked state.

212 -electron microscopy structures of the RNAP, RNAP-TFEalpha binary, and RNAP-TFEalpha-promoter DNA ter

213 occlusion of RNAP binding; (ii) roadblocking RNAP progression; (iii) constraining DNA topology; (iv)

214 ription in part through stabilizing sigma(S)-RNAP by tethering sigma(S) (2) and the beta'CT.

215 lectron microscopy structure of Crl-sigma(S)-RNAP in an open promoter complex with a sigma(S)-regulon

216 We found that C37/53 sensitizes RNAP III termination to RNA:DNA hybrid strength and prom

217 B. subtilis NusG shifts RNAP to the posttranslocation register and induces pausi

218 A similar RNAP II degradation is also evident in mutant ATXN3-expr

219 ibing RNAPs translocate faster than a single RNAP, but their average speed is not altered by large va

220 tly labeled GreB molecules binding to single RNAPs and initiation of individual transcripts from an r

221 complex between the Mycobacterium smegmatis RNAP and HelD.

222 thogenesis involving a virulence-specialized RNAP that employs two (MglA-SspA)-based strategies to ac

223 ter activity, indicating that R. sphaeroides RNAP can utilize -7T when present.

224 nt in E. coli but is required to form stable RNAP-promoter open complexes (RP(o)) and is essential fo

225 tion complex by exerting torque on a stalled RNAP.

226 GreA is characterised to rescue stalled RNAP complexes due to its antipause activity, but also i

227 transcription complexes reactivates stalled RNAPs and dramatically accelerates transcription through

228 We structurally analyzed Bacillus subtilis RNAP-delta-HelD complexes.

229 We found that GreB greatly suppressed RNAP backtracking and remarkably increased the torque th

230 rom uniformly uracilated DNA templates by T7 RNAP indicated an increased frequency of transversion an

231 conditions for in vitro transcription by T7 RNAP were confirmed with this assay, including the impor

232 all possible point mutants of a canonical T7 RNAP promoter, our results coincided well with previous

233 The data for T7 RNAP establishes that even a single dU/A pair can inhibi

234 s optimized for either T7 RNA polymerase (T7 RNAP) or human RNA polymerase II (pol II) have inhibitor

235 After termination, RNAP is thought to initiate the next round of transcript

236 Following termination, RNAP almost always remains bound to DNA and sometimes ex

237 ring the recycling stage, post-terminational RNAPs one-dimensionally diffuse on DNA in downward and u

238 and DNA release are separate steps and that RNAP may remain associated with DNA after termination.

239 We conclude that RNAP clusters are biomolecular condensates that assemble

240 Our results indicate that RNAP and NusA molecules move inside clusters, with mobil

241 We observed that RNAP formed distinct clusters that were engaged in activ

242 The structure reveals that RNAP and BmrR recognize the upstream promoter DNA from o

243 oli Using fluorescence imaging, we show that RNAP quickly transitions from a dispersed to clustered l

244 These results suggest that RNAP was organized into active transcription centers und

245 ing and remarkably increased the torque that RNAP was able to generate by 65%, from 11.2 pN.nm to 18.

246 gating RNA polymerases (RNAPs) and find that RNAPs are likely steric barriers that can push and inter

247 Here we show that RNAPs outpace pioneering ribosomes in the Gram-positive

248 The RNAP-LuxR interaction domain is conserved in Vibrio chol

249 PA induced by nutritional stress, affect the RNAP II C-terminal domain phosphorylation at Ser2, and c

250 Although the RNAP core is catalytically competent for RNA synthesis,

251 or suppress cell-to-cell variability at the RNAP level.

252 structures reveal that TFEalpha bridges the RNAP clamp and stalk domains to open the DNA binding cle

253 opt multiple conformations when bound by the RNAP.

254 We report a method that directly defines the RNAP-active-center position relative to DNA with single-

255 regions of salt-responsive genes drives the RNAP redistribution for reprograming the transcriptome t

256 us, a "nozzle," that narrows and extends the RNAP RNA-exit channel, extruding topologically linked si

257 Cap binds further from the RNAP active site and does not sterically interfere with

258 and DNA from reaching the active site in the RNAP catalytic center.

259 ssembly of human initiation complexes in the RNAP II and RNAP III systems at the single-molecule leve

260 tors, and thus the polymerase itself, in the RNAP III system.

261 Amino acid substitutions in the RNAP interaction domain on LuxR decrease interactions be

262 nscription bubble and loads the DNA into the RNAP active site.

263 actor-like coiled-coil inserts deep into the RNAP secondary channel, dismantling the active site and

264 competition with GreA for insertion into the RNAP secondary channel.

265 p (TL) is a mobile structural element of the RNAP active center that, based on crystal structures, ha

266 known about the role of key elements of the RNAP active site in translesion transcription.

267 l interacts with a structural element of the RNAP beta'-subunit that we call the beta'-clamp-toe (bet

268 To determine the role of the RNAP binding sites in the genome-wide effects of ppGpp o

269 participate in the termination stage of the RNAP II transcription, and preferentially localize to th

270 e cryo-electron microscopy structures of the RNAP, RNAP-TFEalpha binary, and RNAP-TFEalpha-promoter D

271 litating closed-to-open isomerization of the RNAP-promoter complex by compensating for the weak inter

272 a mechanism that apparently is based on the RNAP III transcription level.

273 We find that the two processes require the RNAP-associated factor, DksA.

274 In Bacillus subtilis, the RNAP delta subunit and NTPase HelD have been implicated

275 of RNAP-in restricting access of DNA to the RNAP active site, and explain why clamp opening is requi

276 data from yeast, we investigated whether the RNAP III transcriptional machinery can recruit protein f

277 intaining the TFEalpha interactions with the RNAP mobile modules.

278 e steps of promoter melting occur within the RNAP cleft, delineate key roles for fork-loop 2 and swit

279 This RNAP is resistant to ubiquitous and most regulatory paus

280 We found that this RNAP has very high intrinsic proofreading activity, resu

281 ed in sequence-follows the same path through RNAP as in primary sigma factors, and show that the ECF

282 rge variations in promoter strength and thus RNAP density.

283 regulatory mechanisms, becomes a barrier to RNAP elongation, causing RNAP stalling, backtracking, an

284 ppGpp induction depended on ppGpp binding to RNAP.

285 measure metabolic burden - as it relates to RNAP resource partitioning.

286 locating condensins must bypass transcribing RNAPs within ~1 to 2 s of an encounter at rRNA genes and

287 built-in mechanism by which co-transcribing RNAPs display either collaborative or antagonistic dynam

288 when the promoter is active, co-transcribing RNAPs translocate faster than a single RNAP, but their a

289 ription elongation, in which a translocating RNAP uses a "stepping" mechanism, has been studied exten

290 HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids bin

291 In particular, uncoupled RNAPs in B. subtilis explain the diminished role of Rho-

292 electivity (s) motif specific to PolD versus RNAPs.

293 departed from promoters only in complex with RNAP.

294 sites has a positive linear correlation with RNAP binding at different salt concentrations.

295 methods, we examine how SutA interacts with RNAP and the functional consequences of these interactio

296 The substrate activity of NDPs with RNAP along with those reported for DNA polymerases reinf

297 pecific "pre-termination complex" (PTC) with RNAP and elongation factors NusA and NusG, which stabili

298 y promoting the association of sigma(S) with RNAP without interacting with promoter DNA.

299 omplex, and Q subsequently translocates with RNAP as a pausing-deficient, termination-deficient Q-loa

300 3 is related to heterodimers associated with RNAPs I and II, and C11 is related to TFIIS and Rpa12.2,

301 ould not be expressed since the binding with RNAPs (RNA polymerases) cannot melt the T7 promoter for