ライフサイエンスコーパス: UAA

1 UAAs are incorporated with high specificity, and functio

2 '-GPsiC/3'-CAG, 5'-CPsiG/3'-GAC, 5'-APsiU/3'-UAA and 5'-UPsiA/3'-AAU motifs and their unmodified coun

3 nsferase and either wild type Leu-tRNALeu-4 (UAA) or mutant Leu-tRNALeu-4 (CUA) are each 0.4 +/- 0.2

4 chia coli YoeB toxin interacting with both a UAA stop and an AAU sense codon in pre- and post-mRNA cl

5 l mRNA encoding a tetrapeptide followed by a UAA stop codon and report that initiation factors eIF3,

6 ibited UAA-specific suppressions caused by a UAA-decoding mutant tRNA-Gln (SLT3).

7 GAs in an open reading frame terminated by a UAA.

8 r RF1, tRNA and a messenger RNA containing a UAA stop codon, at 3.2 A resolution.

9 We found that introduction of a UAA stop codon in trpE resulted in a substantial reducti

10 66 was demonstrated by in-cell labeling of a UAA to generate a biosensor for the small GTPase Cdc42.

11 ion, we have mutated the UGA stop codon to a UAA stop codon and to three sense codons that allow cons

12 nd with release factor RF2, in response to a UAA stop codon, solved at 3 A resolution.

13 s the incorporation of unnatural amino acid (UAA) analogues, capable of acting as a label, into the s

14 ny genetically encoded unnatural amino acid (UAA) can be used as a small-molecule attenuator or activ

15 a photo-crosslinkable unnatural amino acid (UAA) cotranslationally incorporated into the parent poly

16 ion of a photoreactive unnatural amino acid (UAA) crosslinking system to capture protein interactions

17 Through multi-site unnatural amino acid (UAA) incorporation, these protein microparticles can als

18 hin living cells using unnatural amino acid (UAA) mutagenesis.

19 ifically introduce the unnatural amino acid (UAA) p-azido-l-phenylalanine (azF) into the intracellula

20 ng genetically encoded unnatural amino acid (UAA) photocross-linkers, p-benzoyl-l-phenylalanine (BzF)

21 netically incorporated unnatural amino acid (UAA) technologies are powerful tools that are greatly en

22 coding a photoreactive unnatural amino acid (UAA).

23 n biosynthesis through unnatural amino acid (UAA*)-mediated suppression of genome-encoded blank codon

24 Unnatural amino acids (UAA) and chemical post-translational modification (cPTM)

25 bility to incorporate unnatural amino acids (UAA) into proteins in a site specific manner can vastly

26 e target selectivity, unnatural amino acids (UAAs) have emerged as critical tools in peptide- and pep

27 ode photocrosslinking unnatural amino acids (UAAs) into 75 different positions in hSERT.

28 ific incorporation of unnatural amino acids (UAAs) into proteins in living cells relies on an enginee

29 cifically incorporate unnatural amino acids (UAAs) into proteins is a powerful tool in protein engine

30 ific incorporation of unnatural amino acids (UAAs) into proteins is a valuable tool for studying stru

31 fically incorporating unnatural amino acids (UAAs) into proteins using engineered E. coli tryptophany

32 bles incorporation of unnatural amino acids (UAAs) into specific sites on the virus capsid.

33 yet unaddressed with unnatural amino acids (UAAs) is whether they can improve the activity of an enz

34 Unnatural amino acids (UAAs) provide a strategy to engineer stringent auxotroph

35 e genetic encoding of unnatural amino acids (UAAs) to overcome this limitation for proteins.

36 n of approximately 70 unnatural amino acids (UAAs) to the genetic codes of Escherichia coli, yeast, a

37 Here, we show that unnatural amino acids (UAAs) with orthogonal chemical reactivity can be used to

38 Fluorescent unnatural amino acids (UAAs), when genetically incorporated into proteins, can

39 eta-substituted unnatural alpha-amino acids (UAAs), which could have a high potential for application

40 After UAA, the mean ratio of EMG-GG to DP decreased to 23% of

41 ug activator nitroreductase activity with an UAA over that of the native active site and a >2.3-fold

42 APyl pairs can simultaneously decode UAG and UAA codons for incorporation of two distinct noncanonica

43 ompetent to terminate translation at UAG and UAA codons, that ribosomes become less efficient at sele

44 reas new tRNAs(Glu) fully cognate to UAG and UAA evolved to reassign these stop codons, the UGA reass

45 ation terminates more efficiently at UAG and UAA than at UGA.

46 ecies that recognize the stop codons UAG and UAA, and ten sense codons.

47 If so, upper-airway anesthesia (UAA) should reduce mechanoreceptor output and therefore

48 red and allowed us to assign most alleles as UAA Allelic differences are primarily located in alpha1

49 tified the insertion of Gln, Tyr, and Lys at UAA and UAG, whereas Trp, Arg, and Cys were inserted at

50 the eRF3 requirement for peptide release at UAA and UAG codons, but not UGA codons.

51 litated efficient translation termination at UAA and UAG codons but not at the UGA codon.

52 ro and in vivo of terminating translation at UAA/UAG codons.

53 nous readthrough, namely Gln, Lys, or Tyr at UAA or UAG PTCs and Trp, Arg, or Cys at UGA PTCs.

54 Incorporation of an azido-UAA enabled site-specific attachment of a cyclic-RGD pep

55 Before UAA, the phasic EMG-GG was linearly related to the defle

56 The full-length eRF1 generated by UAA read-through was present at sub-wild-type levels.

57 acological parameters and the role played by UAAs impact the progress of analogs in preclinical stage

58 tages with an emphasis on the role played by UAAs.

59 systematic study with a variety of clickable UAAs and explored their potential for high-resolution si

60 no evidence to support claims that the codon UAA codes for Tyr in the Platyhelminthes rather than the

61 d glutamine (CAA) to an in-frame stop codon (UAA).

62 However, while the canonical stop codons UAA and UAG are known to be recognized by mtRF1a, the re

63 res the decoding of one of three stop codons UAA, UAG or UGA by the eukaryotic release factor eRF1.

64 on is signaled by any one of the stop codons UAA, UAG, and UGA moving into the ribosomal A site.

65 of three universally conserved stop codons: UAA, UAG or UGA.

66 ced efficiency of termination on the cognate UAA codon.

67 bound peptidyl-tRNA by RF2 reading cognate (UAA and Um6AA) and near-cognate (UAG and Um6AG) stop cod

68 ssitate recognition of only the conventional UAA and UAG termination codons.

69 We demonstrate UAA incorporation by using yeast phenylalanine frameshif

70 f the genetically encoded tryptophan-derived UAAs.

71 tate the incorporation of multiple, distinct UAAs into proteins.

72 timized suppressor plasmids enable efficient UAA incorporation (up to 65% of wild-type levels) into s

73 premature termination codons (PTCs), either UAA, UAG, or UGA.

74 e tRNA and tRNA-Synthetase pairs that enable UAAs incorporation, for use in mammalian systems.

75 These results establish UAA-auxotrophic bacteria as promising candidates for bac

76 we validated the utility of these new (19)F-UAAs as probes for fluorine NMR studies of protein struc

77 structurally related fluorinated UAAs ((19)F-UAAs).

78 low for incorporation of the family of (19)F-UAAs.

79 encodable and polarity-sensitive fluorescent UAA, has been developed.

80 f optically pure L-enantiomer of fluorescent UAAs is crucial for their effective application in live

81 a family of structurally related fluorinated UAAs ((19)F-UAAs).

82 la G73), which has been used extensively for UAA incorporation in Xenopus oocytes.

83 that UAA-NC1 also was recently derived from UAA and translocated from MHC.

84 UDA is distinct from UAA in its differential tissue distribution and its lowe

85 Another nonclassical class I gene (UAA-NC1) was detected that is linked neither to MHC nor

86 estic ducks, we cloned and sequenced genomic UAA-TAP2 fragments from all mallards, which matched tran

87 reas the predominantly expressed MHC class I UAA is not.

88 shark species showed that classical class I (UAA) and class II genes are genetically linked.

89 e found in most vertebrae classical class I (UAA); additionally, the other predicted 28 peptide-bindi

90 is one predominantly expressed MHC class I, UAA, although they have five MHC class I genes in the co

91 RS) must be modified in order to incorporate UAAs into proteins.

92 he standard operating procedure incorporates UAA and cPTM into a "naive" library with 10(8)-10(12) co

93 on is a unique methodology for incorporating UAAs in response to quadruplet codons, but currently, it

94 However, among these only C1054U inhibited UAA-specific suppressions caused by a UAA-decoding mutan

95 f guanosine at position 9 (m(1)G9) of mt-Leu(UAA), while stabilizing the WT tRNA, has a destabilizing

96 Many tRNA(Leu)UAA genes from plastids contain a group I intron.

97 he phylogenetic distribution of the tRNA(Leu)UAA intron follows the clustering of rRNA sequences, bei

98 ur data support the notion that the tRNA(Leu)UAA intron was inherited by cyanobacteria and plastids t

99 ary structural similarities between tRNA(Leu)UAA introns found in strains of the cyanobacterium Micro

100 oes with other known cyanobacterial tRNA(Leu)UAA introns.

101 nterrupt the anticodon loop of the tRNA(Leu)(UAA) gene in a bacterium belonging to the gamma-subdivis

102 teria, and the first instance of a tRNA(Leu)(UAA) group I intron to be found in a group of bacteria o

103 ssing of the genes tRNA(Thr)(UGU), tRNA(Leu)(UAA), and tRNA(Phe) (GAA) therefore attributes the seemi

104 tion of proline analogs and other N-modified UAAs into proteins in E. coli.

105 ll ultimately lead to the appearance of more UAA-charged tRNA.

106 Most UAA alleles have unique residues in the cleft predicting

107 tors showed significant differences in MUAC, UAA and AMA (p < 0.001).

108 aining the mdx premature stop codon mutation UAA (A), which is also the most efficient translational

109 , and many of these are followed with nearby UAA or UGA codons.

110 Neither UAA nor UAG mutations, examined at the same codon positi

111 the need to generate new UaaRSs for many new UAAs.

112 ibility of UAA technology and the use of new UAAs in proteins.

113 ecific suppression of amber (UAG) and ochre (UAA) codons, respectively.

114 hich enhanced suppression by the weak ochre (UAA) suppressor tRNA(Ser) SUQ5.

115 this work will increase the accessibility of UAA technology and the use of new UAAs in proteins.

116 A major limitation to the amount of UAA-containing proteins that can be expressed in the cel

117 expressed in the cell is the availability of UAA-charged orthogonal suppressor tRNA.

118 mbination from the tightly linked cluster of UAA, TAP, and LMP genes, the so-called class I region fo

119 st this hypothesis, we studied the effect of UAA on the relationship between the phasic activity of t

120 fect, but in neither case was readthrough of UAA or UAG observed.

121 e, we outline the strategy and deployment of UAAs in FDA-approved drugs and their targets.

122 While dozens of UAAs have been successfully introduced into proteins exp

123 rotein, via introducing the novel R group of UAAs, that are genetically encoded in the protein's prim

124 ent to which they allow for incorporation of UAAs into protein) and fidelity (the extent to which the

125 he first demonstrations of successful use of UAAs in generating a novel material.

126 The utility of UAAs is illustrated by clinically approved drugs such as

127 duction, respectively. This 6-fold effect on UAA reading was also observed in a single-molecule termi

128 codon, while Euplotes species recognize only UAA and UAG as stop codons.

129 f expression when UGA was replaced by UAG or UAA and the appropriate suppressor was present.

130 he natural tnaC stop codon, UGA, with UAG or UAA in a tnaC-stop codon-tnaA'-'lacZ reporter construct.

131 However, when UAG or UAA replaced UGA, the induced level of expression was al

132 Introducing UAG or UAA stop codons rather than the normal tnaC UGA stop cod

133 en the UGA stop codon was replaced by UAG or UAA, respectively, consistent with the finding that in E

134 reater translational readthrough than UAG or UAA.

135 Recoding of UGA, UAG, or UAA to specify an amino acid allows a proportion of the

136 Insertion of a UGA or UAA codon into the coding region of luciferase abolished

137 te-of-the-art measurements compared to other UAAs.

138 r oligomorphic unlike the highly polymorphic UAA UDA has a low copy number in elasmobranchs but is mu

139 Ribosomes encountering premature UAA or UGA codons in the CAN1 mRNA fail to release and,

140 erine missense substitution at the premature UAA codon.

141 ted, closely linked to a class I pseudogene (UAA-NC2); this region probably resulted from a recent du

142 idine of a premature termination codon (PTC; UAA, UAG or UGA) within an intronless mRNA and U36 of th

143 single location can be sampled very quickly, UAAs can be implemented to improve enzyme active sites a

144 that use the standard genetic code recognize UAA, UAG, and UGA as stop codons, whereas variant code s

145 siae domains 2 and 3 (Eo/Sc eRF1) recognized UAA and UAG, but not UGA, as stop codons.

146 vivo cleavage preference at four sequences (UAA, UAG, UGA, UAC) promotes 5' end stop codons.

147 and specific enrichment of three sequences (UAA, UAG, UGA)-corresponding to stop codons-at piRNA 5'

148 rrently limited to incorporation of a single UAA in response to a stop codon, which is known as nonse

149 s in Escherichia coli MG1655 with synonymous UAA codons, which permitted the deletion of release fact

150 s I genes in the complex, arranged TAP1-TAP2-UAA-UBA-UCA-UDA-UEA The UAA gene, situated proximal to t

151 d in genes expressed at high levels and that UAA serves as the only termination codon.

152 of sequence similarity to UAA suggests that UAA-NC1 also was recently derived from UAA and transloca

153 Insertion of GFP after the UAA-stop was just as effective in increasing Sec inserti

154 orthogonal to the host cell, to deliver the UAA of choice in response to a unique nonsense or frames

155 as aeruginosa to maintain auxotrophy for the UAA p-benzoyl-L-phenylalanine (BzF) through its incorpor

156 In contrast, when pairing the UAA-containing GluN1 subunit with the GluN2A subunit, li

157 ddition to identifying binding partners, the UAA approach maps the binding interface of the bait prot

158 such as the T-loop, the 11-nt receptor, the UAA/GAN and the G-ribo motifs.

159 led a new RNA structural element, termed the UAA/GAN motif.

160 s restored to the UGA mutant, but not to the UAA mutant, upon insertion of the PhGPx 3' UTR.

161 , arranged TAP1-TAP2-UAA-UBA-UCA-UDA-UEA The UAA gene, situated proximal to the TAP2 gene, is express

162 ate amber suppressing tRNAs charged with the UAA.

163 These UAAs represent a wide range of structures and functions

164 We introduced these UAAs at sites throughout the TMD of the GluA2 receptor a

165 site-specifically incorporated two and three UAAs simultaneously into a neuroreceptor expressed in vi

166 mine whether expressed alleles correspond to UAA adjacent to TAP2 as in domestic ducks, we cloned and

167 etected that is linked neither to MHC nor to UAA-NC2; its high level of sequence similarity to UAA su

168 ng of the RF1-specific UAG codon relative to UAA, the universal stop codon, compared with the wild ty

169 C2; its high level of sequence similarity to UAA suggests that UAA-NC1 also was recently derived from

170 e groups were incorporated for attachment to UAAs or small molecules (mero166, azide; mero167, alkyne

171 ationships based on the chloroplast 5'-trnL (UAA)-trnF(GAA) region and estimated divergence times bas

172 E assays, one operating on the plastid trnL (UAA) intron and the other targeting its inner P6 loop in

173 oil: seed oil blends using the plastid trnL (UAA) intron barcode.

174 NA), the LEAFY exon 3 (nrDNA), and the trnL((UAA)) P6 loop (cpDNA).

175 fected messenger RNAs, with the loss of trnL-UAA being particularly severe.

176 sociated with the group I intron in pre-trnL-UAA and group II introns in the ndhA and ycf3 pre-mRNAs.

177 psbZ-trnM-CAU, rps4-trnT-UGU, trnT-UGU-trnL-UAA, ndhC-trnV-UAC, psbE-petL, clpP1, ndhF-rpl32, rpl32-

178 cognizes each of the three stop codons (UAG, UAA, and UGA) and facilitates release of the nascent pol

179 Redefinition of UAG, UAA and UGA to specify a standard amino acid occurs in r

180 cherichia coli glutamine tRNA, suppress UAG, UAA and UGA termination codons, respectively, in a repor

181 factor to one of the three stop codons (UGA, UAA or UAG) results in the termination of protein synthe

182 C-142b, CFC-114, CFC-11, CFC-113) for urban (UAA), rural/remote (RAA), and landfill (LAA) ambient air

183 usly showed domestic ducks predominantly use UAA, one of five MHC class I genes, but whether biased e

184 physicochemical properties in peptides using UAAs.

185 Ochre thus utilizes UAA as the sole stop codon, with UGG encoding tryptophan

186 erties of fluorescent dyes linked to various UAAs for smFRET measurements.

187 was UAG and 3-fold when this stop codon was UAA; basal level expression was reduced by 50% in the co

188 ugh genetic defects at the promoter, whereas UAA and UDA have functionally equivalent promoters.

189 In recent years UAAs have been incorporated in a site-specific manner in