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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 maPFD in the growth and thermal tolerance of M. jannaschii.
7 responsible for generating 6-deoxyhexoses in M. jannaschii.
8 products catalyze Cys-tRNA(Cys) synthesis in M. jannaschii.
9 stent with the higher temperature habitat of M. jannaschii.
10 nvolved in the synthesis of Cys-tRNA(Cys) in M. jannaschii.
11 ratures that are physiologically relevant to M. jannaschii.
12 y source of beta-alanine in cell extracts of M. jannaschii.
13 aschii; and (iii) the use of proteomics with M. jannaschii.
14 istent with the optimal growth conditions of M. jannaschii.
15 me activity is present in the cell lysate of M. jannaschii.
16 ately anaerobic hyperthermophilic methanogen M. jannaschii.
17                             In addition, the M. jannaschii 20S proteasome was purified as a 700-kDa c
18 r H. pylori (5.4%), Synechocystis (4.7%) and M. jannaschii (3.5%) which exhibit substantially lower p
19 roteins, two-thirds of which are shared with M. jannaschii (428 ORFs).
20                               In contrast to M. jannaschii, A. fulgidus has fewer restriction-modific
21 most organisms except for some Archaea (e.g. M. jannaschii, A. fulgidus) and some pathogens (e.g. Hel
22 drive the transcription of two copies of the M. jannaschii aaRS gene.
23                                              M. jannaschii AdoMetDC has a Km of 95 microm and the tur
24 ands that alter the metal specificity of the M. jannaschii agmatinase from Mn(II) to Fe(II).
25                      Therefore, Fsr provides M. jannaschii an anabolic ability and protection from su
26 e a different cysteinyl-tRNA synthetase from M. jannaschii and Deinococcus radiodurans and its charac
27 was also confirmed by using cell extracts of M. jannaschii and Methanosarcina thermophila.
28 5-phospho-D-ribose-1-pyrophosphate (PRPP) in M. jannaschii and other methanogenic archaea.
29                                          (9) M. jannaschii and Synechocystis have a two to threefold
30 ); (ii) experimental functional genomics for M. jannaschii; and (iii) the use of proteomics with M. j
31 . pombe yeast, the E. coli bacterium and the M. jannaschii archaebacterium.
32 n this paper, sequences of 115 proteins from M. jannaschii are compared with their homologs from meso
33 anscription, translation, and replication in M. jannaschii are more similar to those found in Eukaryo
34 production, cell division, and metabolism in M. jannaschii are most similar to those found in Bacteri
35 e possible origins of the thermostability of M. jannaschii AroQf, the smallest natural CM characteriz
36 utants contained portions of ORFs denoted in M. jannaschii as endoglucanase (MJ0555), transketolase (
37               These results suggest that the M. jannaschii as well as related archaeal 20S proteasome
38                      Kinetic analysis of the M. jannaschii aspartate transcarbamoylase from the cell-
39                We propose that ORF MJ1117 of M. jannaschii be annotated as cobY to reflect its involv
40 yo-EM to elucidate the sRNA orientation in a M. jannaschii box C/D di-sRNP.
41                        Thus, the sequence of M. jannaschii can serve as a starting point for gene iso
42 omatography-mass spectrometry analysis of an M. jannaschii cell extract showed the presence of free f
43 yoxal and NADH, NADPH, F 420H 2, or DTT to a M. jannaschii cell extract stimulated the production of
44 d by incorporating 13C into the formate when M. jannaschii cell extracts were incubated with H13CO3-
45 erted into dehydroshikimate and shikimate in M. jannaschii cell extracts, consistent with the remaini
46 CO in reactions catalyzed by A. fulgidus and M. jannaschii cell extracts.
47 tion of the aspartate transcarbamoylase from M. jannaschii cell-free extract revealed that the enzyme
48 city class V aspartate aminotransferase from M. jannaschii converted the phosphohydroxypyruvate produ
49                                 The putative M. jannaschii CorA was expressed in an Mg2+-transport-de
50                    Kinetic studies show that M. jannaschii DHNA possesses a catalytic capability with
51    The predicted ORF MJ1140 in the genome of M. jannaschii encodes ComB, a Mg2+-dependent acid phosph
52                       The genome sequence of M. jannaschii encodes two homologs of each large and sma
53                                 However, the M. jannaschii enzyme has a peptide insertion into its ca
54                              The recombinant M. jannaschii enzyme has a somewhat low, but reasonable
55                                          The M. jannaschii enzyme has been expressed in E. coli and p
56            The bifunctional activity of this M. jannaschii enzyme illustrates the evolution of a supr
57                          The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet
58                             We show that the M. jannaschii enzyme is active on minihelix substrates o
59                        The small size of the M. jannaschii enzyme is due to the absence of most of th
60 nzyme places a stronger emphasis on G35, the M. jannaschii enzyme places a stronger emphasis on G36,
61 fect on the aminoacylation efficiency of the M. jannaschii enzyme.
62                                              M. jannaschii exhibits a slight preference for secondary
63   The overall structural conservation of the M. jannaschii F subunit, although not readily recognizab
64 hes, as well as direct enzymatic assays with M. jannaschii, failed to reveal the presence of PRK.
65                            The difference of M. jannaschii from low-G+C gram-positive proteobacteria
66        An unexpectedly large fraction of the M. jannaschii gene products, 44%, shows significantly hi
67 sequences, orthologues of 25% or less of the M. jannaschii genes were detected in each individual com
68                                    These two M. jannaschii genes were recombinantly expressed in Esch
69 e (SAM) enzymes account for nearly 2% of the M. jannaschii genome, where the major SAM derived produc
70 s of a family with 18 representatives in the M. jannaschii genome.
71 ther anticipated pathway could produce DKFP, M. jannaschii glucose-6-P metabolism was studied in deta
72                        Yet, we observed that M. jannaschii grows and produces methane with sulfite as
73                                    Using the M. jannaschii high-temperature in vitro transcription sy
74  A combination of the homoaconitase with the M. jannaschii homoisocitrate dehydrogenase catalyzed all
75                                          The M. jannaschii homolog of XecG, MJ0255, is located next t
76 ite of the A. fulgidus enzyme and not in the M. jannaschii IMPase, the disruption (e.g., A. fulgidus
77  bacterial genome comparison, are missing in M. jannaschii, indicating massive non-orthologous displa
78 spartate decarboxylase (PanD), the enzyme in M. jannaschii is a pyridoxal phosphate (PLP)-dependent l
79 esults indicate that proline biosynthesis in M. jannaschii is accomplished by a previously unrecogniz
80 oposals that aminoacylation with cysteine in M. jannaschii is an auxiliary function of a canonical pr
81                  The latter functionality in M. jannaschii is assigned to another gene (gi591748), in
82 liminary studies had shown that L-lactate in M. jannaschii is not derived from pyruvate, and thus an
83                            Notably, the free M. jannaschii L7Ae structure is essentially identical to
84                     Furthermore, recombinant M. jannaschii, M. acetivorans, and A. fulgidus RubisCO p
85 ed and efficient comparison of histones from M. jannaschii, Methanosarcina acetivorans (largest Archa
86 ithotrophicus (Mt) and the hyperthermophiles M. jannaschii (Mj) and M. igneus (Mi).
87                   The protein product of the M. jannaschii MJ0400 gene catalyzes the transaldolase re
88 onversion of PRPP to RuBP were identified in M. jannaschii (Mj0601) and Methanosarcina acetivorans (M
89 ated that the protein was the product of the M. jannaschii MJ1025 gene.
90  M. jannaschii prolyl-tRNA synthetase or the M. jannaschii MJ1477 protein provides the "missing" CysR
91                We then tested a hypothetical M. jannaschii O-phosphoseryl-tRNA(Sec) kinase and demons
92                         By using G. lamblia, M. jannaschii, or E. coli tRNA as substrate, this ProRS
93  encode sequences that are >50% identical to M. jannaschii polypeptides, and there is little conserva
94 rs, raised the distinct possibility that the M. jannaschii proline-tRNA synthetase may recruit additi
95                         It was reported that M. jannaschii prolyl-tRNA synthetase or the M. jannaschi
96 these results on the in vivo activity of the M. jannaschii ProRS and on the nature of the enzyme invo
97                                     Although M. jannaschii ProRS catalyzes the synthesis of Cys-tRNA(
98  recent biochemical experiments showing that M. jannaschii ProRS misacylates tRNA(Pro) with cysteine,
99 at pure heterologously expressed recombinant M. jannaschii ProRS misaminoacylates M. jannaschii tRNA(
100 n some respects, recognition of tRNA(Pro) by M. jannaschii ProRS parallels that of human, with a stro
101 es at resolutions between 2.6 and 3.2 A: apo M. jannaschii ProRS, and M. thermautotrophicus ProRS in
102  provide evidence of divergent adaptation by M. jannaschii ProRS; recognition of the tRNA acceptor en
103                             About 53% of the M. jannaschii proteins belong to families of paralogues,
104 each of the bacterial genomes and 73% of the M. jannaschii proteins showed significant sequence simil
105 n contrast, the effector domain of Ptr1, the M. jannaschii Ptr2 paralogue, yields only very weak acti
106  furiosus PurP is structurally homologous to M. jannaschii PurP.
107                                     Only the M. jannaschii PyrB (Mj-PyrB) gene product exhibited cata
108 ion protocol was devised for the Mj-PyrB and M. jannaschii PyrI (Mj-PyrI) gene products.
109 e crystal structure of the SecY channel from M. jannaschii revealed a plug domain that appears to sea
110 eveloped a fluorescently labeled recombinant M. jannaschii RNAP system to probe the archaeal transcri
111 inavir and its analogs inhibit human homolog M. jannaschii S2P cleavage of an artificial protein subs
112                                          The M. jannaschii sequence is unprecedented in its extreme u
113 cked affinity for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate was
114 ures of equivalent plug deletions in SecY of M. jannaschii show that, although the overall structures
115        A second dual-guide box C/D sRNA from M. jannaschii, sR6, also exhibited RNA remodeling during
116                                          The M. jannaschii SSB (mjaSSB) has significant amino acid se
117  the mechanism of Cys-tRNA(Cys) formation in M. jannaschii still remains to be discovered.
118 underrepresented in many thermophiles (e.g., M. jannaschii, Sulfolobus sp., and M. thermoautotrophicu
119                                          The M. jannaschii sulfopyruvate decarboxylase was found to b
120 chaebacterium Methanocaldococcus jannaschii (M. jannaschii), the proteasomal regulatory particle (RP)
121 ophiles are about 50 degrees C below that of M. jannaschii, their genomic G+C contents are nearly ide
122 e cyclodeaminase is present in the genome of M. jannaschii, these results indicate that proline biosy
123 ns, CAU and CAC, by an engineered orthogonal M. jannaschii tRNA with an AUG anticodon: tRNA(Opt) We s
124 me is unable to aminoacylate purified mature M. jannaschii tRNA(Cys) with cysteine in contrast to fac
125  show here that the unmodified transcript of M. jannaschii tRNA(Pro) is indeed mis-acylated with cyst
126 mbinant M. jannaschii ProRS misaminoacylates M. jannaschii tRNA(Pro) with cysteine.
127 ator, and a gene encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expre
128 we show that the gene product of mj0619 from M. jannaschii, which encodes a radical S-adenosylmethion
129 e reductase (RNR) using the recently evolved M. jannaschii Y-tRNA synthetase/tRNA pair.

 
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