ライフサイエンスコーパス: M. jannaschii

1 nsporter closely related to MJ1367-MJ1368 of M. jannaschii.

2 e genomic data of M. thermoautotrophicum and M. jannaschii.

3 ally lacking in H. pylori, Synechocystis and M. jannaschii.

4 s DnaK and DnaJ, which are notably absent in M. jannaschii.

5 as approximately the same number of genes as M. jannaschii.

6 responsible for generating 6-deoxyhexoses in M. jannaschii.

7 products catalyze Cys-tRNA(Cys) synthesis in M. jannaschii.

8 stent with the higher temperature habitat of M. jannaschii.

9 nvolved in the synthesis of Cys-tRNA(Cys) in M. jannaschii.

10 ratures that are physiologically relevant to M. jannaschii.

11 y source of beta-alanine in cell extracts of M. jannaschii.

12 aschii; and (iii) the use of proteomics with M. jannaschii.

13 istent with the optimal growth conditions of M. jannaschii.

14 me activity is present in the cell lysate of M. jannaschii.

15 ately anaerobic hyperthermophilic methanogen M. jannaschii.

16 In addition, the M. jannaschii 20S proteasome was purified as a 700-kDa c

17 r H. pylori (5.4%), Synechocystis (4.7%) and M. jannaschii (3.5%) which exhibit substantially lower p

18 roteins, two-thirds of which are shared with M. jannaschii (428 ORFs).

19 In contrast to M. jannaschii, A. fulgidus has fewer restriction-modific

20 most organisms except for some Archaea (e.g. M. jannaschii, A. fulgidus) and some pathogens (e.g. Hel

21 drive the transcription of two copies of the M. jannaschii aaRS gene.

22 M. jannaschii AdoMetDC has a Km of 95 microm and the tur

23 ands that alter the metal specificity of the M. jannaschii agmatinase from Mn(II) to Fe(II).

24 Therefore, Fsr provides M. jannaschii an anabolic ability and protection from su

25 e a different cysteinyl-tRNA synthetase from M. jannaschii and Deinococcus radiodurans and its charac

26 was also confirmed by using cell extracts of M. jannaschii and Methanosarcina thermophila.

27 5-phospho-D-ribose-1-pyrophosphate (PRPP) in M. jannaschii and other methanogenic archaea.

28 (9) M. jannaschii and Synechocystis have a two to threefold

29 ); (ii) experimental functional genomics for M. jannaschii; and (iii) the use of proteomics with M. j

30 . pombe yeast, the E. coli bacterium and the M. jannaschii archaebacterium.

31 n this paper, sequences of 115 proteins from M. jannaschii are compared with their homologs from meso

32 anscription, translation, and replication in M. jannaschii are more similar to those found in Eukaryo

33 production, cell division, and metabolism in M. jannaschii are most similar to those found in Bacteri

34 e possible origins of the thermostability of M. jannaschii AroQf, the smallest natural CM characteriz

35 utants contained portions of ORFs denoted in M. jannaschii as endoglucanase (MJ0555), transketolase (

36 These results suggest that the M. jannaschii as well as related archaeal 20S proteasome

37 Kinetic analysis of the M. jannaschii aspartate transcarbamoylase from the cell-

38 We propose that ORF MJ1117 of M. jannaschii be annotated as cobY to reflect its involv

39 yo-EM to elucidate the sRNA orientation in a M. jannaschii box C/D di-sRNP.

40 Thus, the sequence of M. jannaschii can serve as a starting point for gene iso

41 omatography-mass spectrometry analysis of an M. jannaschii cell extract showed the presence of free f

42 yoxal and NADH, NADPH, F 420H 2, or DTT to a M. jannaschii cell extract stimulated the production of

43 d by incorporating 13C into the formate when M. jannaschii cell extracts were incubated with H13CO3-

44 erted into dehydroshikimate and shikimate in M. jannaschii cell extracts, consistent with the remaini

45 CO in reactions catalyzed by A. fulgidus and M. jannaschii cell extracts.

46 tion of the aspartate transcarbamoylase from M. jannaschii cell-free extract revealed that the enzyme

47 city class V aspartate aminotransferase from M. jannaschii converted the phosphohydroxypyruvate produ

48 The putative M. jannaschii CorA was expressed in an Mg2+-transport-de

49 Kinetic studies show that M. jannaschii DHNA possesses a catalytic capability with

50 The predicted ORF MJ1140 in the genome of M. jannaschii encodes ComB, a Mg2+-dependent acid phosph

51 The genome sequence of M. jannaschii encodes two homologs of each large and sma

52 However, the M. jannaschii enzyme has a peptide insertion into its ca

53 The recombinant M. jannaschii enzyme has a somewhat low, but reasonable

54 The M. jannaschii enzyme has been expressed in E. coli and p

55 The bifunctional activity of this M. jannaschii enzyme illustrates the evolution of a supr

56 The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet

57 We show that the M. jannaschii enzyme is active on minihelix substrates o

58 The small size of the M. jannaschii enzyme is due to the absence of most of th

59 nzyme places a stronger emphasis on G35, the M. jannaschii enzyme places a stronger emphasis on G36,

60 fect on the aminoacylation efficiency of the M. jannaschii enzyme.

61 M. jannaschii exhibits a slight preference for secondary

62 The overall structural conservation of the M. jannaschii F subunit, although not readily recognizab

63 hes, as well as direct enzymatic assays with M. jannaschii, failed to reveal the presence of PRK.

64 The difference of M. jannaschii from low-G+C gram-positive proteobacteria

65 An unexpectedly large fraction of the M. jannaschii gene products, 44%, shows significantly hi

66 sequences, orthologues of 25% or less of the M. jannaschii genes were detected in each individual com

67 These two M. jannaschii genes were recombinantly expressed in Esch

68 e (SAM) enzymes account for nearly 2% of the M. jannaschii genome, where the major SAM derived produc

69 s of a family with 18 representatives in the M. jannaschii genome.

70 ther anticipated pathway could produce DKFP, M. jannaschii glucose-6-P metabolism was studied in deta

71 Yet, we observed that M. jannaschii grows and produces methane with sulfite as

72 Using the M. jannaschii high-temperature in vitro transcription sy

73 A combination of the homoaconitase with the M. jannaschii homoisocitrate dehydrogenase catalyzed all

74 The M. jannaschii homolog of XecG, MJ0255, is located next t

75 ite of the A. fulgidus enzyme and not in the M. jannaschii IMPase, the disruption (e.g., A. fulgidus

76 bacterial genome comparison, are missing in M. jannaschii, indicating massive non-orthologous displa

77 spartate decarboxylase (PanD), the enzyme in M. jannaschii is a pyridoxal phosphate (PLP)-dependent l

78 esults indicate that proline biosynthesis in M. jannaschii is accomplished by a previously unrecogniz

79 oposals that aminoacylation with cysteine in M. jannaschii is an auxiliary function of a canonical pr

80 The latter functionality in M. jannaschii is assigned to another gene (gi591748), in

81 liminary studies had shown that L-lactate in M. jannaschii is not derived from pyruvate, and thus an

82 Notably, the free M. jannaschii L7Ae structure is essentially identical to

83 Furthermore, recombinant M. jannaschii, M. acetivorans, and A. fulgidus RubisCO p

84 ed and efficient comparison of histones from M. jannaschii, Methanosarcina acetivorans (largest Archa

85 ithotrophicus (Mt) and the hyperthermophiles M. jannaschii (Mj) and M. igneus (Mi).

86 The protein product of the M. jannaschii MJ0400 gene catalyzes the transaldolase re

87 onversion of PRPP to RuBP were identified in M. jannaschii (Mj0601) and Methanosarcina acetivorans (M

88 ated that the protein was the product of the M. jannaschii MJ1025 gene.

89 M. jannaschii prolyl-tRNA synthetase or the M. jannaschii MJ1477 protein provides the "missing" CysR

90 We then tested a hypothetical M. jannaschii O-phosphoseryl-tRNA(Sec) kinase and demons

91 By using G. lamblia, M. jannaschii, or E. coli tRNA as substrate, this ProRS

92 encode sequences that are >50% identical to M. jannaschii polypeptides, and there is little conserva

93 rs, raised the distinct possibility that the M. jannaschii proline-tRNA synthetase may recruit additi

94 It was reported that M. jannaschii prolyl-tRNA synthetase or the M. jannaschi

95 these results on the in vivo activity of the M. jannaschii ProRS and on the nature of the enzyme invo

96 Although M. jannaschii ProRS catalyzes the synthesis of Cys-tRNA(

97 recent biochemical experiments showing that M. jannaschii ProRS misacylates tRNA(Pro) with cysteine,

98 at pure heterologously expressed recombinant M. jannaschii ProRS misaminoacylates M. jannaschii tRNA(

99 n some respects, recognition of tRNA(Pro) by M. jannaschii ProRS parallels that of human, with a stro

100 es at resolutions between 2.6 and 3.2 A: apo M. jannaschii ProRS, and M. thermautotrophicus ProRS in

101 provide evidence of divergent adaptation by M. jannaschii ProRS; recognition of the tRNA acceptor en

102 About 53% of the M. jannaschii proteins belong to families of paralogues,

103 each of the bacterial genomes and 73% of the M. jannaschii proteins showed significant sequence simil

104 n contrast, the effector domain of Ptr1, the M. jannaschii Ptr2 paralogue, yields only very weak acti

105 furiosus PurP is structurally homologous to M. jannaschii PurP.

106 Only the M. jannaschii PyrB (Mj-PyrB) gene product exhibited cata

107 ion protocol was devised for the Mj-PyrB and M. jannaschii PyrI (Mj-PyrI) gene products.

108 e crystal structure of the SecY channel from M. jannaschii revealed a plug domain that appears to sea

109 eveloped a fluorescently labeled recombinant M. jannaschii RNAP system to probe the archaeal transcri

110 inavir and its analogs inhibit human homolog M. jannaschii S2P cleavage of an artificial protein subs

111 The M. jannaschii sequence is unprecedented in its extreme u

112 cked affinity for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate was

113 ures of equivalent plug deletions in SecY of M. jannaschii show that, although the overall structures

114 A second dual-guide box C/D sRNA from M. jannaschii, sR6, also exhibited RNA remodeling during

115 The M. jannaschii SSB (mjaSSB) has significant amino acid se

116 the mechanism of Cys-tRNA(Cys) formation in M. jannaschii still remains to be discovered.

117 underrepresented in many thermophiles (e.g., M. jannaschii, Sulfolobus sp., and M. thermoautotrophicu

118 The M. jannaschii sulfopyruvate decarboxylase was found to b

119 chaebacterium Methanocaldococcus jannaschii (M. jannaschii), the proteasomal regulatory particle (RP)

120 ophiles are about 50 degrees C below that of M. jannaschii, their genomic G+C contents are nearly ide

121 e cyclodeaminase is present in the genome of M. jannaschii, these results indicate that proline biosy

122 ns, CAU and CAC, by an engineered orthogonal M. jannaschii tRNA with an AUG anticodon: tRNA(Opt) We s

123 me is unable to aminoacylate purified mature M. jannaschii tRNA(Cys) with cysteine in contrast to fac

124 show here that the unmodified transcript of M. jannaschii tRNA(Pro) is indeed mis-acylated with cyst

125 mbinant M. jannaschii ProRS misaminoacylates M. jannaschii tRNA(Pro) with cysteine.

126 ator, and a gene encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expre

127 e reductase (RNR) using the recently evolved M. jannaschii Y-tRNA synthetase/tRNA pair.