ライフサイエンスコーパス: RNA triphosphatase

1 iae, this reaction is catalyzed by Cet1p, an RNA triphosphatase.

2 is similarity to the active site of vaccinia RNA triphosphatase.

3 sform it into a strictly manganese-dependent RNA triphosphatase.

4 ce of a carboxylate general acid catalyst in RNA triphosphatase.

5 he guanylyltransferase docking site on yeast RNA triphosphatase.

6 al/viral/protozoal family of metal-dependent RNA triphosphatases.

7 in the absence of its two different types of RNA triphosphatases.

8 talytic mechanism are conserved among fungal RNA triphosphatases.

9 pping of mammalian pre-mRNAs is initiated by RNA triphosphatase, a member of the cysteine phosphatase

10 p formation, a mutant virus that lacked both RNA triphosphatase activities was constructed.

11 S2B-dependent protease, RNA helicase, and 5'-RNA triphosphatase activities.

12 reas the N-terminal part exhibits NTPase and RNA triphosphatase activity and is proposed to have heli

13 truncated derivative Cet1(246-549) also has RNA triphosphatase activity but fails to stimulate Ceg1

14 The RNA triphosphatase activity depends absolutely on a diva

15 sly shown to be essential for vaccinia virus RNA triphosphatase activity inactivated the triphosphata

16 Hence, an RNA triphosphatase activity is essential for eukaryotic

17 RNA triphosphatase activity is optimal at pH 7.5 with ei

18 The RNA triphosphatase activity of Cet1p is magnesium-depend

19 Here, we show that the RNA triphosphatase activity of DUSP11 promotes the RNA s

20 A truncated protein, Cet1(201-549), has RNA triphosphatase activity, heterodimerizes with and st

21 inal region (amino acids 265 to 549) carries RNA triphosphatase activity, while the region containing

22 f LEF-4 but resulted in a modest decrease in RNA triphosphatase activity.

23 The N-terminal domain of CEL-1 has RNA triphosphatase activity.

24 cleopolyhedrovirus encodes two proteins with RNA triphosphatase activity.

25 n N-terminal serine proteinase domain and an RNA triphosphatase, an NTPase domain, and an RNA helicas

26 ns within these motifs are essential for the RNA triphosphatase and ATPase activities of Cet1p in vit

27 their replacement by glutamine abolishes the RNA triphosphatase and ATPase activities.

28 ite nucleophile Cys-119 by alanine abrogates RNA triphosphatase and ATPase activity.

29 capping reactions, which are catalyzed by an RNA triphosphatase and guanylyltransferase.

30 karyotic phylogeny based on the structure of RNA triphosphatase and its physical linkage to the guany

31 The RNA triphosphatase and NTPase activities of baculovirus

32 Concordant mutational inactivation of RNA triphosphatase and nucleoside triphosphatase functio

33 , a bifunctional 597-amino acid protein with RNA triphosphatase and RNA guanylyltransferase activitie

34 on the structure and physical linkage of the RNA triphosphatase and RNA guanylyltransferase enzymes t

35 nosoma brucei consists of separately encoded RNA triphosphatase and RNA guanylyltransferase enzymes.

36 capping enzyme-vaccinia virus D1(1-545)p, an RNA triphosphatase and RNA guanylyltransferase-to functi

37 ted by overexpression of the capping enzymes RNA triphosphatase and RNA guanylyltransferase.

38 een in only three previous structures: yeast RNA triphosphatase and two proteins of unknown function

39 The structure and mechanism of fungal RNA triphosphatases are completely different from those

40 Pct1p and other yeast RNA triphosphatases are completely unrelated, mechanisti

41 that protozoan, fungal, and Chlorella virus RNA triphosphatases belong to a single family of metal-d

42 BVP and other metazoan RNA triphosphatases belong to a superfamily of phosphata

43 ian capping enzyme (Mce1) are members of the RNA triphosphatase branch of the cysteine phosphatase su

44 tructure conservation between members of the RNA triphosphatase branch, whether from cellular or vira

45 PTP/BVP is also an RNA triphosphatase, but is not essential for viral repli

46 ty, and is conserved in the Candida albicans RNA triphosphatase CaCet1p.

47 sists of three components: a 520- amino acid RNA triphosphatase (CaCet1p), a 449-amino acid RNA guany

48 ize that the need for Ceg1p binding by yeast RNA triphosphatase can by bypassed when the triphosphata

49 RNA triphosphatase catalyzes the first step in mRNA cap

50 Saccharomyces cerevisiae RNA triphosphatase Cet1 is an essential component of the

51 cvRtp1 is more similar to that of the yeast RNA triphosphatase Cet1 than it is to the RNA triphospha

52 Saccharomyces cerevisiae RNA triphosphatase (Cet1) and RNA guanylyltransferase (C

53 The 549-amino acid yeast RNA triphosphatase Cet1p catalyzes the first step in mRN

54 The 2.05 A crystal structure of yeast RNA triphosphatase Cet1p reveals a novel active site fol

55 catalytic domain of Saccharomyces cerevisiae RNA triphosphatase Cet1p.

56 Saccharomyces cerevisiae RNA triphosphatase (Cet1p) and RNA guanylyltransferase (

57 The RNA triphosphatases characteristically hydrolyze nucleos

58 The RNA triphosphatase component (CaCet1p) of the mRNA cappi

59 A binding site for the RNA triphosphatase component of the capping apparatus wa

60 iphosphatase enzyme family that includes the RNA triphosphatase component of the mRNA capping apparat

61 CES5 is identical to CET1, which encodes the RNA triphosphatase component of the yeast capping appara

62 Cet1, the RNA triphosphatase component of the yeast mRNA capping a

63 Cet1, the RNA triphosphatase component of the yeast mRNA capping a

64 zosaccharomyces pombe Pct1 are the essential RNA triphosphatase components of the mRNA capping appara

65 structural and mechanistic divergence of the RNA triphosphatase components of the yeast and metazoan

66 These proteins are the 5' RNA triphosphatase Ctl1p, the cell cycle-regulated trans

67 Chlorella virus RNA triphosphatase (cvRtp1) is the smallest member of a

68 of viral replication on an intact nucleotide/RNA triphosphatase domain and an N-terminal cluster of b

69 We recently showed that the RNA triphosphatase domain of the Caenorhabditis elegans

70 AcNPV phosphatase is similar to that of the RNA triphosphatase domain of the metazoan cellular mRNA

71 ific cysteine phosphatases that includes the RNA triphosphatase domains of metazoan and plant mRNA ca

72 We suggest that the metal-dependent RNA triphosphatases encoded by yeast and DNA viruses com

73 hosphatase (BVP) is a member of the metazoan RNA triphosphatase enzyme family that includes the RNA t

74 which is the signature P-loop residue of the RNA triphosphatase family and a likely determinant of th

75 Ctl1 is the second member of the yeast RNA triphosphatase family, but is probably involved in a

76 distinct lineage within the metal-dependent RNA triphosphatase family.

77 y unrelated to the cysteine-phosphatase-type RNA triphosphatases found in metazoans and plants, which

78 y unrelated to the cysteine-phosphatase-type RNA triphosphatases found in metazoans and plants.

79 metal-independent cysteine phosphatase-type RNA triphosphatases found in metazoans and plants.

80 d by the crystal structure of the homologous RNA triphosphatase from Saccharomyces cerevisiae (Cet1p)

81 , or E192A into the fusion protein abrogates RNA triphosphatase function in vivo.

82 ential action of three enzymatic activities: RNA triphosphatase, guanylyl-transferase, and methyltran

83 ls, is catalyzed by the sequential action of RNA triphosphatase, guanylyltransferase, and (guanine-N-

84 Although RNA triphosphatases have a core alpha/beta fold similar

85 RNA triphosphatase is an essential mRNA processing enzym

86 The mechanism of the RNA triphosphatase is similar to that of PTPs: the activ

87 rface is uniquely deleterious when the yeast RNA triphosphatase must function in concert with the end

88 xhibits monomer-associated nucleoside and 5' RNA triphosphatase (NTPase/RTPase) activities that are m

89 A second S. cerevisiae RNA triphosphatase/NTPase (named Cth1p) containing motif

90 e BVP, and were unable to complement a yeast RNA triphosphatase null mutant in vivo.

91 rs mechanistically and structurally from the RNA triphosphatase of mammals.

92 ependent phosphohydrolases that includes the RNA triphosphatases of fungi and other large eukaryotic

93 ependent phosphohydrolases that includes the RNA triphosphatases of fungi and the malaria parasite Pl

94 ependent phosphohydrolases that includes the RNA triphosphatases of fungi, microsporidia, and protozo

95 endent phosphohydrolases, which includes the RNA triphosphatases of fungi, protozoa, Chlorella virus

96 ependent phosphohydrolases that includes the RNA triphosphatases of fungi, protozoa, poxviruses, and

97 turally and mechanistically unrelated to the RNA triphosphatases of metazoans and plants.

98 st RNA triphosphatase Cet1 than it is to the RNA triphosphatases of other DNA viruses.

99 ion of yeast deletion strains missing either RNA triphosphatase or guanylyltransferase required termi

100 fy a novel interaction between fission yeast RNA triphosphatase Pct1, the enzyme that initiates cap f

101 Here we characterize a 303 amino acid RNA triphosphatase (Pct1p) encoded by the fission yeast

102 RNA triphosphatase presents an attractive target for ant

103 Hence, RNA triphosphatase presents an ideal target for structur

104 separate RNA guanylyltransferase (Pgt1) and RNA triphosphatase (Prt1) enzymes and that the triphosph

105 BVP structure to the apoenzyme of mammalian RNA triphosphatase reveals a concerted movement of the A

106 y by the sequential action of three enzymes: RNA triphosphatase, RNA guanylyltransferase, and RNA (gu

107 ing enzyme is a multifunctional protein with RNA triphosphatase, RNA guanylyltransferase, and RNA (gu

108 ere we report that PBCV-1 encodes a separate RNA triphosphatase (RTP) that catalyzes the initial step

109 The RNA triphosphatase (RTPase) activity of NSP2 may account

110 ping enzymes are bifunctional, carrying both RNA triphosphatase (RTPase) and guanylyltransferase (GTa

111 riphosphatase (NTPase)/RNA helicase and a 5'-RNA triphosphatase (RTPase).

112 nistically and structurally, to the metazoan RNA triphosphatases, suggesting an abrupt evolutionary d

113 Trypanosoma brucei RNA triphosphatase TbCet1 is a 252-amino acid polypeptid

114 TP is more similar in structure to the yeast RNA triphosphatases than to the enzymes of metazoan DNA

115 nservation of quaternary structure in fungal RNA triphosphatases, whereby the delicate tunnel archite

116 report the 1.65 A crystal structure of mouse RNA triphosphatase, which reveals a deep, positively cha

117 TbCet1 is a monomeric enzyme, unlike fungal RNA triphosphatases, which are homodimers.

118 t understood family members are the eukaryal RNA triphosphatases, which catalyze the initial step in

119 cal members are the eukaryal metal-dependent RNA triphosphatases, which catalyze the initial step in