ライフサイエンスコーパス: RNAP

1 of cagA expression from a specific sigma(28)-RNAP promoter and consequent induction of the hummingbir

2 The architecture of the 30S*RNAP complex provides a structural basis for co-localiza

3 it to map contacts formed between sigma(70) RNAP holoenzyme from E. coli and the T7A1 promoter, as w

4 lization microscopy to observe the sigma(70)-RNAP complex during initiation from the lambda PR' promo

5 mal conformational changes for accommodating RNAP in the DNA channel, whereas T. maritima sigma1.1 mu

6 ystallized structure of a complete activator/RNAP/DNA complex.

7 hat are either released or extended to allow RNAP to escape from the promoter.

8 escues a severely backtracked RNAP, allowing RNAP to overcome stronger obstacles.

9 We find that although RNAP lacking the gate loop displays moderate defects in

10 ng similarity between sigma1.1 and delta, an RNAP-associated protein in B. subtilis, bearing implicat

11 romoter DNA, unwinds promoter DNA to form an RNAP-promoter open complex (RPo) containing a single-str

12 roximately 13 bp of promoter DNA, forming an RNAP-promoter open complex (RPo) containing a single-str

13 are the TSS profile of WT RNAP to that of an RNAP derivative defective in sequence-specific RNAP-CRE

14 AP, RPOTp-the plastidial RNAP, and RPOTmp-an RNAP active in both organelles.

15 the subsequent coordination between Mfd and RNAP have remained elusive.

16 rkably delicate coordination between Mfd and RNAP, allowing efficient targeting and recycling of Mfd

17 and reveals the interactions between TAP and RNAP holoenzyme responsible for transcription activation

18 Escherichia coli RNAP, the Thermus aquaticus RNAP/DNA complex, AsiA /sigma(70) Region 4, the N-termin

19 ross the DNA binding channel of the archaeal RNAP.

20 eviously hypothesized paused and backtracked RNAP initiation intermediate and suggest it is biologica

21 cktracking or rescues a severely backtracked RNAP, allowing RNAP to overcome stronger obstacles.

22 Using a bacterial RNAP containing the alternative sigma(54) factor and cry

23 the mechanism of TSS selection by bacterial RNAP and suggest a general mechanism for TSS selection b

24 nce of the sigma-RNAP interface in bacterial RNAP function and regulation and potentially for interve

25 potently and selectively inhibits bacterial RNAP in vitro, inhibits bacterial growth in culture, and

26 ccessive motions of the initiating bacterial RNAP by studying real-time signatures of fluorescent rep

27 vRNAP does not contain homologs of bacterial RNAP alpha subunits, it contains, in addition to the bet

28 ll protein to specifically perturb bacterial RNAP activity in exponentially growing Escherichia coli.

29 o conditions that directly perturb bacterial RNAP performance can result in a biphasic growth behavio

30 s the productive engagement of the bacterial RNAP containing the major variant bacterial sigma factor

31 hat either modulate or inhibit the bacterial RNAP to allow the temporal regulation of bacteriophage g

32 olves interaction with DNA and the bacterial RNAP.

33 uired for its accommodation within bacterial RNAP.

34 Bacterial RNAPs were proposed to rely on the same mobile element o

35 hus represents a novel type of bacteriophage RNAPs.

36 tions within transcription complexes between RNAP, transcription factors, and nucleic acids that allo

37 nsistent with functional interaction between RNAP and the 30S subunit.

38 e structure reveals the interactions between RNAP holoenzyme and DNA responsible for transcription in

39 rotein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in di

40 We propose that an interaction between RNAPs via the torque produced by RNAP motion on helicall

41 tors to RNA cleavage reportedly vary between RNAPs from different bacterial species and, probably, di

42 tural framework to understand how Nun blocks RNAP translocation, we determined structures of Escheric

43 tment at the FLO1 promoter still occurs, but RNAP II is absent from the gene-coding region, demonstra

44 However, transcription directed by RNAP I to III was suppressed by M.

45 ion between RNAPs via the torque produced by RNAP motion on helically twisted DNA can explain this ap

46 A polymerase (RNAP) function is regulated by RNAP-associated protein factors.

47 eased initiation-to-elongation transition by RNAP.

48 by pauses, which has been observed to cause RNAP traffic jams; yet some studies indicate that elonga

49 We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit.

50 we determined structures of Escherichia coli RNAP ternary elongation complexes (TECs) with and withou

51 y determined 3D structures (Escherichia coli RNAP, the Thermus aquaticus RNAP/DNA complex, AsiA /sigm

52 proofreading hydrolysis by Escherichia coli RNAP.

53 y crystal structures of the Escherichia coli RNAPs containing the most clinically important S531L mut

54 Here, by comparing RNAPs from Escherichia coli, Deinococcus radiodurans, an

55 losed complex into a catalytically competent RNAP-promoter open complex.

56 RNA polymerase by simultaneously contacting RNAP and the ntDNA strand.

57 recruitment to gene promoters and decreased RNAP II C-terminal domain (CTD) Ser2 phosphorylation dur

58 reA-dependent cleavage are lower for DeltaTL RNAP variants, suggesting that the TL contributes to the

59 regulate transcription by the DNA-dependent RNAP.

60 he viral RNA conformations that occur during RNAP binding and initial replication.

61 drolysis are controlled in part by a dynamic RNAP component called the trigger loop (TL), which cycle

62 ted phage 82 Q protein (82Q) can also engage RNAP that is paused at a promoter-distal position and th

63 Ordinarily, Q engages RNAP during early elongation when it is paused at a spec

64 Our findings establish RNAP-CRE interactions are a functional determinant of TS

65 ction by bacterial, archaeal, and eukaryotic RNAP.

66 As a result, delta facilitates RNAP to initiate transcription in the second scale, comp

67 positive bacteria, especially in fermicutes, RNAP is associated with an additional factor, called del

68 We demonstrate that YonO is a bona fide RNAP of the SPbeta bacteriophage that specifically trans

69 -binding channel where it locks the flexible RNAP clamp in one position.

70 nced an E. coli genomic library enriched for RNAP-binding RNAs.

71 boxyl-terminal domain, which is required for RNAP-ribosome interaction in vitro and for pronounced ce

72 verlaps with the respective binding site for RNAP.

73 to backtracked complexes or is ejected from RNAP by catalytic turnover.

74 ow that NusA-AR2 is able to remove NusG from RNAP.

75 The properties of generated RNAP variants revealed an RNA/protein interaction networ

76 represses transcription initiation from host RNAP-dependent promoters on the phage genome via a mecha

77 tion, the phage protein P7 inhibits the host RNAP by preventing the productive engagement with the pr

78 time that the major variant form of the host RNAP can also be targeted by bacteriophage-encoded trans

79 Our findings explain how RNAP thermal motions control the promoter search and dri

80 Our structures show how RNAP-sigma(54) interacts with promoter DNA to initiate t

81 umulate in nucleoli during RNA polymerase I (RNAP I) transcription.

82 expression requires that RNA Polymerase II (RNAP II) gain access to DNA in the context of chromatin.

83 ustrated that M inhibited RNA polymerase II (RNAP II) recruitment to gene promoters and decreased RNA

84 As (miRNAs) derived from RNA polymerase III (RNAP III) transcribed precursors.

85 RNA polymerase III (RNAP III) type III promoters (U6 or H1) are typically us

86 ing to significant conformational changes in RNAP and sigma(54) that promote RPo formation.

87 tood, the roles of conformational changes in RNAP are less well described.

88 profile of the RNAP derivative defective in RNAP-CRE interactions differed from that of WT RNAP, in

89 PUM inhibits RNAP through a binding site on RNAP (the NTP addition si

90 During transcription initiation RNAP remains associated with the upstream promoter DNA v

91 archaea as its presence on all genes matches RNAP.

92 by ppGpp involves promotion of UvrD-mediated RNAP backtracking.

93 scue, and its short residence time minimizes RNAP inhibition.

94 ge-type RNA polymerases RPOTm (mitochondrial RNAP), RPOTp (plastidial RNAP), and RPOTmp (active in bo

95 ee phage-type RNAPs, RPOTm-the mitochondrial RNAP, RPOTp-the plastidial RNAP, and RPOTmp-an RNAP acti

96 We observe the interaction of the Msm RNAP alpha-subunit C-terminal domain (alphaCTD) with DNA

97 s)-that potently and selectively inhibit Mtb RNAP and Mtb growth, and we report crystal structures of

98 ify an Mtb-specific structural module of Mtb RNAP and establish that Rif functions by a steric-occlus

99 wth, and we report crystal structures of Mtb RNAP in complex with AAPs.

100 We report crystal structures of Mtb RNAP, alone and in complex with Rif, at 3.8-4.4 A resolu

101 AAPs bind to a different site on Mtb RNAP than Rif, exhibit no cross-resistance with Rif, fun

102 ems to be faster in the presence of multiple RNAPs than elongation by a single RNAP.

103 assemble into two non-canonical multisubunit RNAPs - a virion RNAP (vRNAP) that is injected into the

104 tions of RMP with three common RIF(R) mutant RNAPs suggests that modifications to RMP may recover its

105 clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycoba

106 Many natural RNAP-binding aptamers, termed RAPs, were mapped to the g

107 In addition, the novel RNAP/RT inhibitors are characterized by a potent antibac

108 ir binding to promoter DNA in the absence of RNAP, and when in complex with RNAP, it occupies the DNA

109 e SC and reprogram the catalytic activity of RNAP, but the dynamics of these factors' interactions wi

110 rvation of omega and its role in assembly of RNAP, E. coli mutants lacking rpoZ (codes for omega) are

111 omega) are viable due to the association of RNAP with the global chaperone protein GroEL.

112 ons did, however, affect the backtracking of RNAP necessary for proofreading and potentially the reac

113 RNAP, it occupies the DNA-binding channel of RNAP.

114 The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting differen

115 P3T4S5P6S7 heptapeptide repeat of the CTD of RNAP II in Schizosaccharomyces pombe by substituting non

116 The C-terminal domain (CTD) of RNAP II recruits chromatin modifying enzymes to promoter

117 uencing, 5' mNET-seq, we assessed effects of RNAP-CRE interactions at natural promoters in Escherichi

118 end readout, MASTER, we assessed effects of RNAP-CRE interactions on TSS selection in vitro and in v

119 g structures was observed upon inhibition of RNAP I transcription.

120 a second identified here at an interface of RNAP and the transcription factor DksA (site 2).

121 h in turn are responsible for the loading of RNAP into the transcription units.

122 The occupancies of RNAP and Spt4/5 strongly correlate with each other and w

123 ies by altering the initiation properties of RNAP.

124 of defining the structural rearrangements of RNAP that are involved in the two mechanisms of transcri

125 and was shown to be involved in recycling of RNAP at the end of each round of transcription.

126 ay, we show that delta-mediated recycling of RNAP cannot be the sole reason for the enhancement of tr

127 ently shown, in addition to the recycling of RNAP, delta functions as a transcriptional activator by

128 iptional factors with even small segments of RNAP can alter promoter specificity.

129 ng how a mutation within the beta subunit of RNAP (G1249D), which is far removed from AsiA or MotA, i

130 hought that delta functioned as a subunit of RNAP to enhance the level of transcripts by recycling RN

131 The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the

132 Active elongation of RNAPs is often interrupted by pauses, which has been obs

133 ts suggest that the torsional interaction of RNAPs is an important mechanism in maintaining fast tran

134 the so-far unknown binding site of delta on RNAP.

135 s for ppGpp enhancement of DksA's effects on RNAP.

136 le if any structural or functional impact on RNAP in the absence of RIF.

137 ignatures of fluorescent reporters placed on RNAP and DNA in the presence of ligands locking the clam

138 PUM inhibits RNAP through a binding site on RNAP (the NTP addition site) and mechanism (competition

139 rained downstream DNA duplex within the open RNAP active site cleft.

140 close, and it has been assumed that the open RNAP separates promoter DNA strands and then closes to e

141 s of its properties, we have re-named ORF145 RNAP Inhibitory Protein (RIP).

142 POTm (mitochondrial RNAP), RPOTp (plastidial RNAP), and RPOTmp (active in both organelles) to recogni

143 the mitochondrial RNAP, RPOTp-the plastidial RNAP, and RPOTmp-an RNAP active in both organelles.

144 larity between the bacterial RNA polymerase (RNAP) "switch region" and the viral non-nucleoside rever

145 at directly targets the host RNA polymerase (RNAP) and efficiently represses its activity.

146 itor that inhibits bacterial RNA polymerase (RNAP) and exhibits antibacterial activity against drug-r

147 Here we show that RNA polymerase (RNAP) and the ribosome of Escherichia coli can form a de

148 direct interactions between RNA polymerase (RNAP) and the translational machinery.

149 , thought to be a subunit of RNA polymerase (RNAP) and was shown to be involved in recycling of RNAP

150 rut site promotes pausing of RNA polymerase (RNAP) at a single Rho-dependent termination site over 10

151 xpression and the removal of RNA polymerase (RNAP) at the ends of transcription units.

152 S531 of Escherichia coli RNA polymerase (RNAP) beta subunit is a part of RNA binding domain in tr

153 Upon RNA polymerase (RNAP) binding to a promoter, the sigma factor initiates

154 ng transcription initiation, RNA polymerase (RNAP) binds to promoter DNA, unwinds promoter DNA to for

155 inhibition of the bacterial RNA polymerase (RNAP) by the 7 kDa T7 protein Gp2.

156 ompete to associate with the RNA polymerase (RNAP) core enzyme to form a holoenzyme that is required

157 RNA polymerase (RNAP) expedites the recognition of DNA damage by NER com

158 During each of these stages, RNA polymerase (RNAP) function is regulated by RNAP-associated protein f

159 ate transcription by binding RNA polymerase (RNAP) holoenzyme and competing with promoter DNA.

160 al contacts made between the RNA polymerase (RNAP) holoenzyme and promoter DNA modulate not only the

161 ng transcription initiation, RNA polymerase (RNAP) holoenzyme unwinds approximately 13 bp of promoter

162 ing a CAP dimer, a sigma(70)-RNA polymerase (RNAP) holoenzyme, a complete class I CAP-dependent promo

163 omoter DNA template and with RNA polymerase (RNAP) holoenzyme.

164 ly related to the eukaryotic RNA polymerase (RNAP) II system, while archaeal genomes are more similar

165 In bacteria, RNA polymerase (RNAP) initiates transcription by synthesizing short tran

166 The Escherichia coli RNA polymerase (RNAP) is a multisubunit protein complex containing the s

167 The mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosi

168 tion process, the elongating RNA polymerase (RNAP) is dislodged from the DNA template either at speci

169 RNA cleavage by RNA polymerase (RNAP) is the central step in co-transcriptional RNA proo

170 Mtb RNA polymerase (RNAP) is the target of the first-line antituberculosis d

171 The single-subunit RNA polymerase (RNAP) of bacteriophage T7 is able to perform all steps o

172 Bacterial RNA polymerase (RNAP) requires sigma factors to recognize promoter seque

173 al transcription initiation, RNA polymerase (RNAP) selects a transcription start site (TSS) at variab

174 n elongation factor binds to RNA polymerase (RNAP) soon after transcription initiation and dissociati

175 mammalian cells using split RNA polymerase (RNAP) tags.

176 s to examine the kinetics of RNA polymerase (RNAP) transcription initiation in greater detail.

177 coliphage lambda by stalling RNA polymerase (RNAP) translocation specifically on lambda DNA.

178 to the secondary channel of RNA polymerase (RNAP) using interactions similar, but not identical, to

179 that MglA-SspA, which binds RNA polymerase (RNAP), also interacts with the C-terminal domain of PigR

180 m the RpoB S531L mutation in RNA polymerase (RNAP), has become a growing problem worldwide.

181 sites 60 A apart on E. coli RNA polymerase (RNAP), one characterized previously (site 1) and a secon

182 Both bind to RNA polymerase (RNAP), regulating pausing as well as intrinsic and Rho-d

183 t stimulates RNA cleavage by RNA polymerase (RNAP), the functions of lineage-specific Gfh proteins re

184 via direct interaction with RNA polymerase (RNAP), we deep sequenced an E. coli genomic library enri

185 The bacterial RNA polymerase (RNAP), which catalyzes transcription, can thus be consid

186 isomerization of an initial RNA polymerase (RNAP)-promoter closed complex into a catalytically compe

187 promoter specificity to the RNA polymerase (RNAP).

188 a weak RNA-DNA hybrid within RNA polymerase (RNAP).

189 beta' subunits of bacterial RNA polymerase (RNAP).

190 d by the viral RNA-dependent RNA polymerase (RNAP).

191 the initiation properties of RNA polymerase (RNAP).

192 elongation factor that binds RNA polymerase (RNAP).

193 itiation by Escherichia coli RNA polymerase (RNAP; alpha2betabeta'omegasigma(70)), we compare product

194 RECQ5 DNA helicase binds to RNA-polymerase (RNAP) II during transcription elongation and suppresses

195 Most bacterial RNA polymerases (RNAP) contain five conserved subunits, viz.

196 hannel (SC) of multisubunit RNA polymerases (RNAPs) allows access to the active site and is a nexus f

197 Single-subunit RNA polymerases (RNAPs) are present in phage T7 and in mitochondria of al

198 lution-related multisubunit RNA polymerases (RNAPs) carry out RNA synthesis in all domains life.

199 dislodgement by elongating RNA polymerases (RNAPs) from the target promoter, or able to be a strong

200 active site of multisubunit RNA polymerases (RNAPs) is highly conserved from humans to bacteria.

201 e in Escherichia coli, many RNA polymerases (RNAPs) transcribe the DNA simultaneously.

202 he coordinated interplay of RNA polymerases (RNAPs) with nucleic acids and transcription factors.

203 All cellular RNA polymerases (RNAPs), from those of bacteria to those of man, possess

204 eferentially act on stalled RNA polymerases (RNAPs).

205 scription is carried out by RNA polymerases (RNAPs).

206 to the ppGpp binding site in the DksA-ppGpp-RNAP complex.

207 Furthermore, we showed that Mfd prevents RNAP backtracking or rescues a severely backtracked RNAP

208 pstream DNA and how the interactions recruit RNAP.

209 nhance the level of transcripts by recycling RNAP.

210 y which SC factors may cooperate to regulate RNAP while minimizing mutual interference.

211 By rendering RNAP backtracking-prone, ppGpp couples transcription to

212 able data and our results for representative RNAPs.

213 in the absence of H3K14 acetylation reveals RNAP II recruitment at the FLO1 promoter still occurs, b

214 trinsic termination pathway, the role of Rho-RNAP interactions in Rho-dependent termination, and the

215 In RPo, RNAP core enzyme makes sequence-specific protein-DNA int

216 rther underscore the importance of the sigma-RNAP interface in bacterial RNAP function and regulation

217 f multiple RNAPs than elongation by a single RNAP.

218 e, we investigated whether sequence-specific RNAP-CRE interactions affect TSS selection.

219 AP derivative defective in sequence-specific RNAP-CRE interactions.

220 -interest is tagged with an N-terminal split RNAP (RNAPN), and multiple potential binding partners ar

221 The split RNAP tags improve upon other protein fragment complement

222 main of PigR, thus anchoring the (MglA-SspA)-RNAP complex to the FPI promoter.

223 proach to RbpA and show that RbpA stabilizes RNAP-promoter open complexes (RPo) via a distinct mechan

224 fficiently patrol DNA for frequently stalled RNAPs.

225 fluorescently labeled recombinant 12-subunit RNAP system with single-molecule FRET measurements.

226 port the error rates of three single-subunit RNAPs measured from the catalytic efficiencies of correc

227 datively damaged DNA by three single-subunit RNAPs provides the basic information to understand the e

228 lly redundant in mammalian cells to suppress RNAP I transcription-associate R-loops.

229 The average error rates of T7 RNAP (2 x 10(-6)), yeast mitochondrial Rpo41 (6 x 10(-6)

230 rates in mitochondria and, in the case of T7 RNAP, to assess the quality of in vitro transcribed RNAs

231 ners are each fused to orthogonal C-terminal RNAPs (RNAPC).

232 TFS4 destabilises the TBP-TFB-RNAP pre-initiation complex and inhibits transcription i

233 We propose that RNAP-CRE interactions modulate the position of the downs

234 mbination with gel-based assays, showed that RNAP exit kinetics from complexes stalled at later stage

235 ide the RNAP active site cleft suggests that RNAP clamp opening is required for Nun to establish its

236 The RNAP-ribosome interface includes the RNAP subunit alpha

237 In addition, the RNAP-GreA endonuclease accelerated transcription kinetic

238 TSS, the RNAP leading-edge position, and the RNAP trailing-edge position.

239 TEC by taking advantage of gaps between the RNAP and the nucleic acids.

240 acid scaffold, essentially crosslinking the RNAP and the nucleic acids to prevent translocation, a m

241 along the mRNA and eventually dislodges the RNAP via an unknown mechanism.

242 resistance is excessive, Mfd dissociates the RNAP, clearing the DNA for other processes.

243 f 30 nucleotides of mRNA extending from the RNAP active center to the ribosome decoding center.

244 usly displaces the sigma(70) factor from the RNAP.

245 h the 3' terminus of the viral RNA is in the RNAP active site.

246 nt RNA structure and the trigger loop in the RNAP active site.

247 Changes in the RNAP leading-edge position, but not the RNAP trailing-ed

248 hairpin after invasion of the hairpin in the RNAP main cleft.

249 ant sigma factor interacting surfaces in the RNAP substantially overlap, but different regions of sig

250 The RNAP-ribosome interface includes the RNAP subunit alpha carboxyl-terminal domain, which is re

251 the RNAP beta and beta' subunits inside the RNAP active site cleft as well as with nearly every elem

252 The nature of Nun interactions inside the RNAP active site cleft suggests that RNAP clamp opening

253 cleic acids that allosterically modulate the RNAP during the transcription cycle.

254 the RNAP leading-edge position, but not the RNAP trailing-edge position, are a defining hallmark of

255 that even in the absence of nucleotides, the RNAP-bound 3' termini of both vRNA and cRNA exist in two

256 of a subset of conformational states of the RNAP as they exist in crystals.

257 re of an Actinobacteria-unique insert of the RNAP beta' subunit.

258 ational changes of the flexible clamp of the RNAP by combining a fluorescently labeled recombinant 12

259 and we observed that the TSS profile of the RNAP derivative defective in RNAP-CRE interactions diffe

260 addition site) that differ from those of the RNAP inhibitor and current antibacterial drug rifampin (

261 are: (i) forward and reverse movement of the RNAP leading edge, but not trailing edge, relative to DN

262 her by binding directly to the region of the RNAP secondary channel that otherwise binds ppGpp, and i

263 ibe a unifying model for the function of the RNAP TL, which reconciles available data and our results

264 tor directly compromises the activity of the RNAP?

265 active process initiated in RPc and that the RNAP conformations of intermediates are significantly di

266 le-stranded template DNA is delivered to the RNAP active site.

267 h should replace the TL to get access to the RNAP active site.

268 0) and sigma(54) are used for binding to the RNAP, our results further underscore the importance of t

269 ry of 4(10) promoter sequences, the TSS, the RNAP leading-edge position, and the RNAP trailing-edge p

270 apping an unstable intermediate in which the RNAP contacts with the nontemplate strand discriminator

271 C-terminal segment of Nun interacts with the RNAP beta and beta' subunits inside the RNAP active site

272 how AsiA/MotA redirects sigma, and therefore RNAP activity, to T4 promoter DNA, and demonstrate at a

273 te activator protein (CAP)], T. thermophilus RNAP sigma(A) holoenzyme, a class II TAP-dependent promo

274 r, or able to be a strong roadblock to these RNAPs.

275 This RNAP class plays important roles in biotechnology and ce

276 y impair intrinsic RNA cleavage by all three RNAPs and eliminate the interspecies differences in the

277 All three RNAPs exhibit a distinctly high propensity for GTP misin

278 Our observation that delta does not bind to RNAP holo enzyme but is required to bind to DNA upstream

279 ract with ppGpp in DksA, and TraR binding to RNAP uses the residues in the beta' rim helices that con

280 Even though it binds to RNAP with only slightly higher affinity than DksA and is

281 Binding of NusG to RNAP does not require interaction with RNA.

282 nscription, including recruitment of NusG to RNAP, resynchronization of transcription:translation cou

283 Using cytological profiling, tracking RNAP behavior at single-molecule level and transcriptome

284 s through its interactions with transcribing RNAP and through regions of sequence-complementarity wit

285 Thus, also in plant phage-type RNAPs the specificity loop is engaged in promoter recogn

286 cotyledonous plants possess three phage-type RNAPs, RPOTm-the mitochondrial RNAP, RPOTp-the plastidia

287 A factors activate RNA cleavage by wild-type RNAPs to similar levels.

288 rence is due to an altered conformation upon RNAP binding or to differences in intrinsic properties b

289 microRNA (miRNA) gene architecture that uses RNAP III type II promoters.

290 non-canonical multisubunit RNAPs - a virion RNAP (vRNAP) that is injected into the host along with p

291 anscribe early phage genes, and a non-virion RNAP (nvRNAP), which is synthesized during the infection

292 oli, and we identified 39 promoters at which RNAP-CRE interactions determine TSS selection.

293 coli, sigma(70), can remain associated with RNAP during the transition from initiation to elongation

294 lable: from Escherichia coli in complex with RNAP and from T. maritima solved free in solution.

295 rus (ATV) forms a high-affinity complex with RNAP by binding inside the DNA-binding channel where it

296 he absence of RNAP, and when in complex with RNAP, it occupies the DNA-binding channel of RNAP.

297 dynamics of these factors' interactions with RNAP and how they function without cross-interference ar

298 tabilizing protein-protein interactions with RNAP holoenzyme.

299 approaches to compare the TSS profile of WT RNAP to that of an RNAP derivative defective in sequence

300 AP-CRE interactions differed from that of WT RNAP, in a manner that correlated with the presence of c