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1 S. coelicolor A3(2), M600 and J1501 possess L-TIRs, wher
2 S. coelicolor membranes were also able to catalyse the t
3 S. coelicolor mutants globally deficient in antibiotic p
4 S. coelicolor PecS, which exists as a homodimer, binds t
5 S. coelicolor PNPase was more effective than its E. coli
6 S. coelicolor produces SapB, an amphipathic peptide that
7 S. coelicolor shows a bias toward one type of genetic in
8 her characterize the Amycolatopsis sp. AA4 - S. coelicolor interaction by examining expression of dev
10 d near the RNase ES termini interact with an S. coelicolor homologue of polynucleotide phosphorylase
11 minal region of RbpA and sigma domain 2, and S. coelicolor RbpA mutants that are defective in binding
13 x range of -450 to +80 mV, P. aeruginosa and S. coelicolor SoxR are less sensitive to viologens, whic
15 of colony biofilms in both P. aeruginosa and S. coelicolor, which shows that "secondary metabolites"
16 s possible to predict operons in E. coli and S. coelicolor with 83% and 93% accuracy respectively, us
18 hat the Streptomyces species S. lividans and S. coelicolor, morphologically complex gram-positive soi
20 n both the S. coelicolor parental strain and S. coelicolor YL/sgFabH (a deltafabH mutant carrying a p
21 t, we screened FGEs from M. tuberculosis and S. coelicolor against synthetic peptide libraries and id
23 surfactin acts antagonistically by arresting S. coelicolor aerial development and causing altered exp
26 o-ACP was phosphopantetheinylated to 100% by S. coelicolor holo-acyl carrier protein synthase (ACPS),
29 s to find that deferrioxamine E, produced by S. coelicolor, could be readily utilized by Amycolatopsi
32 e development of aerial hyphae and spores by S. coelicolor is inhibited by surfactin, a lipopeptide s
35 removed or duplicated hundreds of contiguous S. coelicolor genes, altering up to 33% of the chromosom
36 C3 were shown to restore to a SapB-deficient S. coelicolor mutant the capacity to undergo complete mo
37 xtracellular signalling cascade proposed for S. coelicolor and is a member of the bldD extracellular
39 Our data suggests a comprehensive role for S. coelicolor AfsS as a master regulator of both antibio
42 r structural zinc, the RbpA orthologues from S. coelicolor and M. tuberculosis share a common structu
47 active precursor, modulates SoxR activity in S. coelicolor to stimulate the production of a membrane
49 first time the presence of albaflavenone in S. coelicolor and clearly demonstrate that the biosynthe
52 vious studies of prodiginine biosynthesis in S. coelicolor support a novel role for RedJ in facilitat
53 al activator of actinorhodin biosynthesis in S. coelicolor, is inhibited by the binding of heptaene,
58 metabolism and morphological development in S. coelicolor and the identification of host-encoded lea
59 n production or morphological development in S. coelicolor, although their mutation could influence t
62 onCI, encoding a flavin-linked epoxidase, in S. coelicolor was shown to significantly increase the ab
64 ed were substrates, including those found in S. coelicolor extracts, and all yielded several products
67 x reductase (FDR) proteins coded by genes in S. coelicolor were expressed in Escherichia coli, purifi
68 lly, coexpressing the rifG-N and -J genes in S. coelicolor YU105 under the control of the act promote
71 n M. tuberculosis and critical for growth in S. coelicolor, these data support a model in which RbpA
72 dence that many of the targets identified in S. coelicolor are also under the control of the sigmaR h
73 th 76% amino acid identity was identified in S. coelicolor, and insertional mutagenesis indicated tha
74 is the third ACP to have been identified in S. coelicolor; the two previously characterized ACPs are
75 are consistent with duplication of GCH II in S. coelicolor promoting evolution of a new function.
77 ferring rifampin-resistance, was isolated in S. coelicolor to provide a genetic marker to follow tran
79 tibiotics and other secondary metabolites in S. coelicolor, suggest that revision of the currently pr
80 rated by the absence of RamS modification in S. coelicolor hyphae treated with the Bacillus subtilis
81 coelicolor, it normally is expressed only in S. coelicolor-generating the deep-blue colonies responsi
82 ly increase the database of known operons in S. coelicolor and provide valuable information for explo
84 RNA increases during the stationary phase in S. coelicolor and that induction of a plasmid-borne copy
87 under the control of its native promoter in S. coelicolor M512, a host lacking the SCP1 plasmid, and
91 w that a representative of these proteins in S. coelicolor possesses a dodecameric quaternary structu
95 [3H]-adenosine were used to label the RNA in S. coelicolor cultures of different ages, and total RNA
97 re color, showing that disruption of sigF in S. coelicolor changes the nature of the spore pigment ra
104 tionally mutated library was introduced into S. coelicolor, and transposon insertions were recovered
107 d that a 4.9 Mb central region of the linear S. coelicolor chromosome encodes 'core' functions expres
111 ore genes were downregulated when grown near S. coelicolor, leading us to find that deferrioxamine E,
112 report the genome sequence of PhiCAM, a new S. coelicolor generalized transducing bacteriophage, iso
113 own to significantly increase the ability of S. coelicolor to epoxidize linalool, a model substrate f
114 oarrays to measure globally the abundance of S. coelicolor transcripts in cells growing in liquid med
115 ift assays revealed an increased affinity of S. coelicolor PNPase for the substrate possessing a 3' s
116 chromatography/mass spectrometry analysis of S. coelicolor culture extracts established the presence
118 as also capable of restoring the capacity of S. coelicolor and S. tendae bald mutants to erect aerial
120 During stationary phase, the composition of S. coelicolor transcripts appears to shift from large qu
121 chain elongation intermediate to cultures of S. coelicolor CH999/pJRJ2 results in formation of a 16-m
123 rbpA expression is induced upon exposure of S. coelicolor to rifampicin and that this, in part, invo
128 with our previous demonstration that ftsZ of S. coelicolor is not needed for viability, these finding
130 omoters changed over the course of growth of S. coelicolor and studies in three sigma factor mutant s
131 genes expressed during vegetative growth of S. coelicolor cultures, we used DNA microarrays to measu
132 tively constant over the course of growth of S. coelicolor M145, but that on a molar basis, the level
133 alin A (ConA) inhibited phi C31 infection of S. coelicolor J1929, and this could be partially reverse
137 tions, construction of a sigF null mutant of S. coelicolor M145 caused the same change in spore color
138 that all of the characterized bld mutants of S. coelicolor are defective in the regulation of galP1,
140 cedure for generating insertional mutants of S. coelicolor based on in vitro transposition of a plasm
147 t Streptomyces lividans, a close relative of S. coelicolor and naturally Pgl-, does not contain homol
148 Addition of the gamma-butyrolactone SCB1 of S. coelicolor resulted in loss of the DNA-binding abilit
149 al and essential sigma factor (sigmaHrdB) of S. coelicolor restored Act and Red production in the afs
151 -Seq, we have examined the transcriptomes of S. coelicolor M145 and an RNase III (rnc)-null mutant of
153 ing to the approximate mass of the predicted S. coelicolor msdA product (52.6 kDa), and specific MSDH
155 ion of a pentapeptide (HCDLP) to recombinant S. coelicolor NiSOD lacking these N-terminal residues, N
157 two phylogenetically distant streptomycetes, S. coelicolor A3(2) and S. griseus: (1) gamma -butyrolac
158 perature and osmotic upshifts, we found that S. coelicolor transiently induces a set of several hundr
162 in vitro and in vivo experiments showed that S. coelicolor ParB protein interacts specifically with t
167 predominate (approximately 70%) in both the S. coelicolor parental strain and S. coelicolor YL/sgFab
168 tion of differentiation-related mRNAs by the S. coelicolor AbsB/RNase III enzyme occurs largely by ri
169 lated globally and differentially during the S. coelicolor growth cycle by the RNaseIII homologue Abs
173 rth protein was sought and purified from the S. coelicolor CH999 host on the basis of its ability to
174 isolated SigT-interactive proteins from the S. coelicolor lysate based on the tandem affinity purifi
175 st other members of this class, however, the S. coelicolor bkdR gene product serves to repress transc
177 re 57 putative GntR family regulators in the S. coelicolor genome) that respond to nutritional and/or
178 for an uridylyltransferase) are found in the S. coelicolor genome, the regulation of the GSI activity
184 d to be glycosylated with a trihexose in the S. coelicolor parent strain, J1929, but not in the pmt(-
186 Unlike the E. coli soxR deletion mutant, the S. coelicolor equivalent is not hypersensitive to oxidan
187 of the predicted amino acid sequence of the S. coelicolor beta' subunit to those characterized from
188 ted mutagenesis, the carboxy terminus of the S. coelicolor beta' subunit was modified to contain six
190 kinetics, and protein crystallography of the S. coelicolor enzyme, we have now identified the +1 to +
192 gene (fabD) encoding another subunit of the S. coelicolor FAS, malonyl coenzyme A:ACP acyl-transfera
194 rresponding to the 4.9 Mb core region of the S. coelicolor M145 chromosome were more highly expressed
197 beta' subunits, one of which consists of the S. coelicolor subunit and those from Mycobacterium lepra
198 f the cleavage sites in the stem-loop of the S. coelicolor transcript are more akin to those identifi
199 those obtained by microarray analysis of the S. coelicolor transcriptome and with studies describing
200 acin and ramoplanin were not inducers of the S. coelicolor VanRS system, in contrast to results obtai
201 s of genes immediately adjacent to it on the S. coelicolor chromosome that likely encode an ATP-bindi
202 We exploited this distinction to replace the S. coelicolor vanRS genes with the vanRS genes from S. t
203 ination, indicating the possibility that the S. coelicolor promoter/activator functions appropriately
204 lmL), which exhibits a low similarity to the S. coelicolor SerRS, is hypothesized to play a role in v
207 ted interchange of this residue in the three S. coelicolor intragenomic homologues is necessary and s
209 levels changed by >/= 2-fold between the two S. coelicolor strains and organized those transcripts in
212 triketide 6, compounds 18, 31, and 32, with S. coelicolor CH999/pJRJ2, resulting in the formation of
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