ライフサイエンスコーパス: UGA codon

1 factor and tRNA(Sec) needed to reassign the UGA codon.

2 in binding also prevented readthrough of the UGA codon.

3 ts specific incorporation is directed by the UGA codon.

4 ational incorporation of selenocysteine at a UGA codon.

5 al and collaborated in Sec insertion at each UGA codon.

6 he compounding effect of termination at each UGA codon.

7 a provided that it is spatially close to the UGA codon.

8 ial of the SECIS flanking region and the Sec UGA codon.

9 stem loop starting six nucleotides 3' of the UGA codon.

10 ementary to the region downstream of the Sec UGA codon.

11 ination at UAA and UAG codons but not at the UGA codon.

12 dant enzyme by promoting substitution at the UGA codon.

13 mino acid selenocysteine, as directed by the UGA codon.

14 er polypeptide chain, encoded by an in-frame UGA codon.

15 carboxyl terminus and which is encoded by a UGA codon.

16 terminate at the second, third, and seventh UGA codons.

17 itive to antibiotics due to its ten in frame UGA codons.

18 proximately 10-fold at subsequent downstream UGA codons.

19 ynthesis but cannot decode the mitochondrial UGA codons.

20 ptide release at UAA and UAG codons, but not UGA codons.

21 and distinct roles for SECIS1 and SECIS2 at UGA codons.

22 in vertebrates may contain up to 22 in-frame UGA codons.

23 the coding regions immediately downstream of UGA codons.

24 ife by dynamic translational redefinition of UGA codons.

25 any of these are followed with nearby UAA or UGA codons.

26 l insertion of selenocysteine in response to UGA codons.

27 rders magnitude, and that termination at the UGA codon abolishes activity.

28 n initiation, structures located adjacent to UGA codons, additional coding sequence regions necessary

29 15) was identified that contains an in-frame UGA codon and a SECIS element in the 3'-UTR.

30 A UGA codon and a selenocysteine insertion sequence in the

31 as most selenoprotein mRNAs contain a single UGA codon and a single SECIS element, selenoprotein P ge

32 nation of translation at the second in-frame UGA codon and all of the 10 in-frame UGA codons being re

33 loop RNA structure immediately following the UGA codon and forms part of the coding sequence in bacte

34 (Sec) tRNA (tRNA([Ser]Sec)) decodes specific UGA codons and contains i(6)A.

35 to the primary sequence arrangement between UGA codons and SECIS elements, their proximity within th

36 nthesis and insertion of Cys into protein at UGA codons and suggest new biological functions for thio

37 from Metridium senile that has four in-frame UGA codons and two nearly identical SECIS elements.

38 tion RNA structures, the coding potential of UGA codons, and the presence of cysteine-containing homo

39 teine Insertion Sequence (SECIS) element and UGA codon are sufficient for selenocysteine (Sec) insert

40 n the 3'-untranslated region and an in-frame UGA codon are the requisite cis-acting elements for the

41 The in-frame UGA codons are recoded to cotranslationally incorporate

42 s by translational recoding whereby in-frame UGA codons are redefined to encode the selenium containi

43 of selenoproteins requires the decoding of a UGA codon as selenocysteine (Sec) instead of translation

44 In eukaryotes, the decoding of the UGA codon as selenocysteine (Sec) requires a Sec inserti

45 that the percentage of ribosomes decoding a UGA codon as selenocysteine rather than termination can

46 ncorporation (i.e., after decoding the first UGA codon as selenocysteine) are fully competent to term

47 The decoding of specific UGA codons as selenocysteine is specified by the Sec ins

48 odon, which allows decoding of mitochondrial UGA codons as tryptophan.

49 ntain a selenocysteine residue, encoded by a UGA codon, as the penultimate carboxyl-terminal amino ac

50 on model that incorporated Sec at non-native UGA codons at rates equal to those of endogenous glutath

51 n-frame UGA codon and all of the 10 in-frame UGA codons being read through to produce Se-P57B.

52 -nucleotide-long fragments representing each UGA codon context into a luciferase reporter construct h

53 verexpressing eRF1 and eRF3, and of altering UGA codon context, on the efficiency of selenoprotein sy

54 One of the UGA codons corresponded to the conserved catalytic Sec o

55 the inefficient incorporation of Sec at the UGA codon during mRNA translation augments the nonsense-

56 Sec or Cys in MsrBs, whereas the three other UGA codons evolved recently and had no homologs with Sec

57 chain as compared with selenocysteine at the UGA codon, expression of the catalytically inactive Gpx4

58 Unlike Mycoplasma cells, which use the UGA codon for tryptophane, Prochlorococcus uses the stan

59 -kDa GFP/GPX1 proteins, Sec incorporation at UGA codons, formerly close to the 5' or 3' ends, was inc

60 SECIS elements recode UGA codons from "stop" to "sense." These RNA secondary s

61 ASec) drives the recoding of highly specific UGA codons from stop signals to Sec.

62 ertion systems probably decode only a single UGA codon in C.elegans and C.briggsae genomes.

63 (6%) translational redefinition of the SEPN1 UGA codon in human cells.

64 They raise the possibility that the second UGA codon in selenoprotein P mRNA can have alternative f

65 uence element approximately 4.8 kb 3' to the UGA codon in the active center and three short open read

66 ocated adjacent to a selenocysteine-encoding UGA codon in the eukaryal gene, SEPN1.

67 first is a conserved, inefficiently decoded UGA codon in the N-terminal region, which appears to ser

68 Sec is encoded by a UGA codon in the selenoprotein mRNA.

69 Selenocysteine (Sec) is incorporated at UGA codons in mRNAs possessing a Sec insertion sequence

70 Cys was inserted in vivo at UGA codons in natural mammalian TRs, and this process wa

71 c) is site-specifically delivered at defined UGA codons in selenoprotein mRNAs.

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

73 djacent to, or near, selenocysteine-encoding UGA codons in the Sps2, SelH, SelO, and SelT selenoprote

74 e conductance regulator (CFTR) W1282X PTC (a UGA codon) in the context of its three upstream and down

75 ocysteine incorporation element along with a UGA codon into a reporter construct allows for read-thro

76 Selenocysteine incorporation at the first UGA codon is inefficient but increases by approximately

77 on of selenocysteine (Sec) into protein, the UGA codon is transformed from one that signals translati

78 ocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion seque

79 steine incorporation as the distance between UGA codons is increased, and that efficient selenocystei

80 rected by translational recoding of specific UGA codons located upstream of a stem-loop structure kno

81 proteins via the translational recoding of a UGA codon, normally used as a stop signal.

82 ec incorporation at the first and downstream UGA codons occurs with variable efficiencies to control

83 D helix in ribosomes stalled at the in-frame UGA codon of prfB generates tension on the mRNA that des

84 hate led to targeted insertion of Cys at the UGA codon of thioredoxin reductase 1 (TR1).

85 G read-through element upstream of the first UGA codon or by providing a competing messenger RNA in t

86 was to systematically examine the effect of UGA codon position on efficiency of Sec insertion.

87 that Sec is more efficiently incorporated at UGA codons positioned in the middle of the coding region

88 proximately 31 kDa and contains two in-frame UGA codons presumably encoding selenocysteine.

89 ts direct incorporation of selenocysteine at UGA codons, provided the SECIS element lies a sufficient

90 UGA codon reassignment renders SR1 genes untranslatable

91 he stem (G1922) is specifically critical for UGA codon recognition by the class 1 release factor RF2.

92 ocysteine (Sec) into proteins in response to UGA codons requires a cis-acting RNA structure, Sec inse

93 Selenocysteine incorporation at UGA codons requires cis-acting mRNA secondary structures

94 Sec specification by UGA codons requires the presence of a cis-acting selenoc

95 t immediately upstream and downstream of the UGA codon significantly affects termination to incorpora

96 75)Se labeling showed that all four in-frame UGA codons supported Sec insertion and that both SECIS e

97 atter was due to termination at the internal UGA codon that codes for selenocysteine.

98 nic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal st

99 lutathione peroxidase 1 (Se-GPx1) contains a UGA codon that is recognized as a codon for the nonstand

100 ec-tRNA(Sec)) to the ribosome and suppresses UGA codons that are upstream of Sec insertion sequence (

101 diated decay due to the presence of in-frame UGA codons that can be decoded as either selenocysteine

102 co-translationally incorporated at specific UGA codons that normally serve as termination signals.

103 fic expansion of the genetic code allows for UGA codons to specify the amino acid selenocysteine (Sec

104 Briefly, conversion of the three UGA codons to UGG codons was required to obtain full-len

105 on in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes

106 When the UGA codon was changed to the Trp codon UGG, flagellar as

107 Although the major readthrough event at the UGA codon was insertion of tryptophan, Sec was also inco

108 n immediately downstream of the Sec-encoding UGA codon, whereas in eukaryotes a completely different

109 e the unusual amino acid selenocysteine at a UGA codon, which conventionally serves as a termination

110 of selenoprotein messages by redefinition of UGA codons, which normally specify termination of transl

111 In selenoprotein mRNAs, UGA codons, which typically specify termination, serve a

112 3' UTR of selenoprotein genes and recodes a UGA codon within the coding sequence.

113 n, we used a reporter gene system that has a UGA codon within the protein-coding region of the lucife

114 is inserted cotranslationally in response to UGA codons within selenoprotein mRNAs in a process requi