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1 rthermophilic methanogen, Methanocaldococcus jannaschii.
2  S2P metalloprotease from Methanocaldococcus jannaschii.
3  and syntrophic coculture with Methanococcus jannaschii.
4 mino acid biosynthesis in Methanocaldococcus jannaschii.
5 ponsible for generating 6-deoxyhexoses in M. jannaschii.
6 mologous E/F complex from Methanocaldococcus jannaschii.
7 ed and characterized from Methanocaldococcus jannaschii.
8 Clostridium difficile and Methanocaldococcus jannaschii.
9 a subunits from the methanogen Methanococcus jannaschii.
10 NA polymerase (RNAP) from Methanocaldococcus jannaschii.
11 pathway leading to DHQ in Methanocaldococcus jannaschii.
12 ducts catalyze Cys-tRNA(Cys) synthesis in M. jannaschii.
13  extracts of the archaeon Methanocaldococcus jannaschii.
14 nt with the higher temperature habitat of M. jannaschii.
15 lved in the synthesis of Cys-tRNA(Cys) in M. jannaschii.
16 ures that are physiologically relevant to M. jannaschii.
17 Methanosarcina thermophila and Methanococcus jannaschii.
18 thermoautotrophicum, M. thermophila, and Mc. jannaschii.
19 hyperthermophilic euryarchaeon Methanococcus jannaschii.
20  DHNA from the methanogen Methanocaldococcus jannaschii.
21 case from the hyperthermophile Methanococcus jannaschii.
22 oserine phosphatase (PSP) from Methanococcus jannaschii.
23 ized from the hyperthermophile Methanococcus jannaschii.
24 hii; and (iii) the use of proteomics with M. jannaschii.
25 ource of beta-alanine in cell extracts of M. jannaschii.
26 aeoglobus fulgidus, and Methanocaldocococcus jannaschii.
27 egulatory protein, GlnK1, from Methanococcus jannaschii.
28 the thermophilic archaeon Methanocaldococcus jannaschii.
29 romoters in the genome of Methanocaldococcus jannaschii.
30 the fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution.
31 t organisms except for some Archaea (e.g. M. jannaschii, A. fulgidus) and some pathogens (e.g. Helico
32 studied the Trx system of Methanocaldococcus jannaschii--a deeply rooted hyperthermophilic methanogen
33 ve the transcription of two copies of the M. jannaschii aaRS gene.
34                                           M. jannaschii AdoMetDC has a Km of 95 microm and the turnov
35 s that alter the metal specificity of the M. jannaschii agmatinase from Mn(II) to Fe(II).
36 richia coli using evolved Methanocaldococcus jannaschii aminoacyl-tRNA synthetase(s) (aaRS)/suppresso
37  atlantica, Alteromonas sp., Marinobacterium jannaschii, Amphritea japonica) were incubated in autocl
38                   Therefore, Fsr provides M. jannaschii an anabolic ability and protection from sulfi
39  MJ1541 gene product from Methanocaldococcus jannaschii, an enzyme that was annotated as a 5'-methylt
40   In contrast, the IMPase from Methanococcus jannaschii, an organism in which DIP does not accumulate
41 emained nearly intact in the Marinobacterium jannaschii and Amphritea japonica incubations.
42 Escherichia coli, archaea like Methanococcus jannaschii and animal viruses.
43 hereas ThrRS enzymes from Methanocaldococcus jannaschii and Archaeoglobus fulgidus were not.
44 er I-1-Pases (from the archaea Methanococcus jannaschii and Archaeoglobus fulgidus, and from the bact
45  different cysteinyl-tRNA synthetase from M. jannaschii and Deinococcus radiodurans and its character
46 gonal aaRSes derived from Methanocaldococcus jannaschii and Escherichia coli tyrosyl-tRNA synthetases
47 terium thermoautotrophicum and Methanococcus jannaschii and in Bacillus subtilis.
48  the genomes of Archae such as Methanococcus jannaschii and Methanobacterium thermoautotrophicum has
49 he transcription factor IIB of Methanococcus jannaschii and Methanocaldococcus vulcanius, revealing a
50 ophicus, and hyperthermophiles Methanococcus jannaschii and Methanococcus igneus were studied to dete
51  also confirmed by using cell extracts of M. jannaschii and Methanosarcina thermophila.
52  The methanogenic archaea Methanocaldococcus jannaschii and Methanothermobacter thermautotrophicus co
53 that mimicked the RPAs in Methanocaldococcus jannaschii and Methanothermobacter thermautotrophicus th
54  enzymes from the archaea Methanocaldococcus jannaschii and Methanothermobacter thermautotrophicus, f
55 , its operon organization with Methanococcus jannaschii and Methanothermobacter thermoautotrophicum.
56  homologues were found in Methanocaldococcus jannaschii and Methanothermobacter thermoautotrophicus,
57 hown that Methanocaldococcus (Methanococcus) jannaschii and other anaerobic archaea synthesize cataly
58 hospho-D-ribose-1-pyrophosphate (PRPP) in M. jannaschii and other methanogenic archaea.
59 aeolicus,47 Bacillus subtilis, Methanococcus jannaschii and Pseudomonas aeruginosa that provide stron
60 GC-rich regions in the AT-rich Methanococcus jannaschii and Pyrococcus furiosus genomes efficiently d
61 erthermophilic marine archaeon Methanococcus jannaschii and shown to catalyze the final reactions in
62 haea, including the methanogen Methanococcus jannaschii and the sulfate-reducing archaeon Archaeoglob
63 s of the F and P subunits from Methanococcus jannaschii and used them in in vitro and in vivo protein
64 ethanococcus maripaludis, Methanocaldococcus jannaschii, and Sulfolobus solfataricus.
65 (ii) experimental functional genomics for M. jannaschii; and (iii) the use of proteomics with M. jann
66 omes and whole-cell lysates of Methanococcus jannaschii (approximately 1,800 genes) using a 2D protei
67 ombe yeast, the E. coli bacterium and the M. jannaschii archaebacterium.
68 ort, it is shown not only that Methanococcus jannaschii, Archaeoglobus fulgidus, Methanosarcina aceti
69 , have been identified in Methanocaldococcus jannaschii as the enzymes involved in the synthesis of D
70 the methanogenic archaeon Methanocaldococcus jannaschii as well as most methanogens, none of the expe
71  of a specificity subunit from Methanococcus jannaschii at 2.4-A resolution.
72  structure of the complex from Methanococcus jannaschii at a resolution of 3.2 A.
73  the sequenced genomes of Methanocaldococcus jannaschii, Bacillus cereus ATCC 10987 and Methylococcus
74             We propose that ORF MJ1117 of M. jannaschii be annotated as cobY to reflect its involveme
75 EM to elucidate the sRNA orientation in a M. jannaschii box C/D di-sRNP.
76 and circular forms) using Methanocaldococcus jannaschii box C/D RNP core proteins.
77 /D sRNP from the archaeon Methanocaldococcus jannaschii by single-particle electron microscopy.
78  the related MjNhaP1 from Methanocaldococcus jannaschii can be attributed to an additional negatively
79 the tyrosyl-tRNA synthetase of Methanococcus jannaschii can be used to genetically encode unnatural a
80 chaeal Sulfolobus shibatae and Methanococcus jannaschii CCA-adding enzymes, are also capable of poly(
81 tography-mass spectrometry analysis of an M. jannaschii cell extract showed the presence of free form
82 al and NADH, NADPH, F 420H 2, or DTT to a M. jannaschii cell extract stimulated the production of bot
83 y incorporating 13C into the formate when M. jannaschii cell extracts were incubated with H13CO3- and
84 ed into dehydroshikimate and shikimate in M. jannaschii cell extracts, consistent with the remaining
85 in reactions catalyzed by A. fulgidus and M. jannaschii cell extracts.
86 n of the aspartate transcarbamoylase from M. jannaschii cell-free extract revealed that the enzyme ha
87 rmophiles Aquifex aeolicus and Methanococcus jannaschii complement enteric amtB mutants for growth at
88 of FAICAR synthetase from Methanocaldococcus jannaschii complexed with various ligands, including the
89 e hyperthermophilic methanogen Methanococcus jannaschii contains homologs of most genes required for
90 y class V aspartate aminotransferase from M. jannaschii converted the phosphohydroxypyruvate product
91                 Kinetic studies show that M. jannaschii DHNA possesses a catalytic capability with a
92 totypical NBD MJ0796 from Methanocaldococcus jannaschii dimerizes in response to ATP binding and diss
93 at of non-nitrogen fixing Methanocaldococcus jannaschii DSM 2661.
94 esponding fragment of the Methanocaldococcus jannaschii Elp3 protein.
95 ic, methanogenic archaeon Methanocaldococcus jannaschii encodes a CobY protein (Mj CobY) that transfe
96 that the MJ0438 gene from Methanocaldococcus jannaschii encodes a novel S-adenosylmethionine-dependen
97 yperthermophilic archaeon Methanocaldococcus jannaschii encodes a potent transcriptional activator, P
98 The predicted ORF MJ1140 in the genome of M. jannaschii encodes ComB, a Mg2+-dependent acid phosphata
99                    The genome sequence of M. jannaschii encodes two homologs of each large and small
100 The hyperthermophilic archaeon Methanococcus jannaschii encodes two putative transcription regulators
101 The hyperthermophilic archaeon Methanococcus jannaschii encodes two putative transcription regulators
102  the C-terminal domain of Methanocaldococcus jannaschii endonuclease.
103   Here we report that the Methanocaldococcus jannaschii enzyme derived from the MJ0309 gene is an Fe(
104         The bifunctional activity of this M. jannaschii enzyme illustrates the evolution of a suprafa
105 me places a stronger emphasis on G35, the M. jannaschii enzyme places a stronger emphasis on G36, a f
106 (67), and Cys(272) in the Methanocaldococcus jannaschii enzyme) are essential for the sulfhydrylation
107 an end product of the purified recombinant M.jannaschii enzyme.
108 , as well as direct enzymatic assays with M. jannaschii, failed to reveal the presence of PRK.
109 teins from the methanogen Methanocaldococcus jannaschii formed the first homoaconitase shown to catal
110                            The Methanococcus jannaschii gene MJ0671 was cloned and overexpressed in E
111                           Methanocaldococcus jannaschii gene MJ1179 encodes a protein that is classif
112 +C)% screening alone, a 1% fraction of the M.jannaschii genome containing all 44 known transfer RNAs,
113 d archaeal protein in the Methanocaldococcus jannaschii genome, MJ0887, which could be involved in th
114 SAM) enzymes account for nearly 2% of the M. jannaschii genome, where the major SAM derived products
115 r anticipated pathway could produce DKFP, M. jannaschii glucose-6-P metabolism was studied in detail
116                     Yet, we observed that M. jannaschii grows and produces methane with sulfite as th
117  enzymes, the hyperthermophile Methanococcus jannaschii has an enzyme, DCD-DUT, that harbors both dCT
118 yde dehydrogenase (ASADH) from Methanococcus jannaschii has been determined to 2.3 angstroms resoluti
119  The riboflavin kinase in Methanocaldococcus jannaschii has been identified as the product of the MJ0
120 hyperthermophilic euryarchaeon Methanococcus jannaschii has no recognizable homologues of the canonic
121 The hyperthermophilic archaeon Methanococcus jannaschii has two members of this gene family.
122 yde and hydroxyacetone in Methanocaldococcus jannaschii have been established.
123               Cell extracts of Methanococcus jannaschii have been shown to readily convert L-ornithin
124 yses of the F(420)s present in Methanococcus jannaschii have shown that these cells contain a series
125 se encoded by the ComA gene in Methanococcus jannaschii have suggested that ComA, which catalyzes the
126                                 Using the M. jannaschii high-temperature in vitro transcription syste
127 combination of the homoaconitase with the M. jannaschii homoisocitrate dehydrogenase catalyzed all of
128                                       The M. jannaschii homolog of XecG, MJ0255, is located next to a
129  syn conformation reported for Methanococcus jannaschii homoserine kinase.
130  high-resolution structures of Methanococcus jannaschii HSK ternary complexes with its amino acid sub
131 nduced the ordered oligomer of Methanococcus jannaschii Hsp16.5 to transition to either expanded symm
132  an engineered variant of Methanocaldococcus jannaschii Hsp16.5 wherein a 14 amino acid peptide from
133  from that of zinc-loaded Methanocaldococcus jannaschii HypB as well as subtle changes to the protein
134  of the A. fulgidus enzyme and not in the M. jannaschii IMPase, the disruption (e.g., A. fulgidus IMP
135 he structure of KsgA from Methanocaldococcus jannaschii in complex with several ligands, including th
136  from the archaebacterium Methanocaldococcus jannaschii in its free form (2.2 A resolution) and bound
137 ere observed in (G+C)% and, in Methanococcus jannaschii, in the frequency of the dinucleotide 'CG'.
138 with the related organism Methanocaldococcus jannaschii included the absence of inteins, even though
139 rresponding activity from Methanocaldococcus jannaschii indicated that tRNA(Cys) becomes acylated wit
140  known structure, MJ0796, from Methanococcus jannaschii indicates that at least two binding sites par
141                           Methanocaldococcus jannaschii is a hypertheromphilic, strictly hydrogenotro
142      AdoMetDC from the Archaea Methanococcus jannaschii is a prototype for a recently discovered clas
143 rtate decarboxylase (PanD), the enzyme in M. jannaschii is a pyridoxal phosphate (PLP)-dependent l-as
144 lts indicate that proline biosynthesis in M. jannaschii is accomplished by a previously unrecognized
145 sals that aminoacylation with cysteine in M. jannaschii is an auxiliary function of a canonical proly
146           The enzyme from Methanocaldococcus jannaschii is designated MptA to indicate that it cataly
147 19 gene in the methanogen Methanocaldococcus jannaschii is likely this missing methylase.
148 inary studies had shown that L-lactate in M. jannaschii is not derived from pyruvate, and thus an alt
149 us putative gene (MJ1604) from Methanococcus jannaschii is now annotated as a phosphofructokinase, wh
150             Whereas ProRS from Methanococcus jannaschii is similar to E. coli in its ability to hydro
151 zyme encoded by Mj0883 of Methanocaldococcus jannaschii is the archaeal counterpart of the bacterial
152  the hyperthermophilic Archaea Methanococcus jannaschii, is a member of the small heat-shock protein
153 th isoprene biosynthesis, Methanocaldococcus jannaschii isopentenyl phosphate kinase is predicted to
154 iae, Escherichia coli and Methanocaldococcus jannaschii It presents the following data: (i) hierarchi
155 s demonstrate that recombinant Methanoccocus jannaschii L7 protein binds the box C/D snoRNA core moti
156  The crystal structure of Methanocaldococcus jannaschii L7Ae has been determined to 1.45 A, and L7Ae'
157                         Notably, the free M. jannaschii L7Ae structure is essentially identical to th
158 ir highest Blastp hits in Methanocaldococcus jannaschii, lateral gene transfer or gene loss has appar
159 talytic residue from a related Methanococcus jannaschii LonB, also faces the solvent and does not int
160    In the archaebacterium Methanocaldococcus jannaschii (M. jannaschii), the proteasomal regulatory p
161                  Furthermore, recombinant M. jannaschii, M. acetivorans, and A. fulgidus RubisCO poss
162 and efficient comparison of histones from M. jannaschii, Methanosarcina acetivorans (largest Archaeal
163 ic and non-halophilic Archaea (Methanococcus jannaschii, Methanosarcina mazei, Methanobrevibacter smi
164   However, the genomes of Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, and
165 ve not been identified in Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, or M
166 heat-shock protein (sHSP) from Methanococcus jannaschii (Mj HSP16.5) forms a homomeric complex of 24
167 e complex of the archaeal Methanocaldococcus jannaschii (Mj) Ago.
168        The interaction of Methanocaldococcus jannaschii (Mj) Nop56/58 with the methyltransferase fibr
169 opentenyl kinase (IPK) in Methanocaldococcus jannaschii (MJ) suggests a new variation of the MVA path
170 RNA splicing endonuclease from Methanococcus jannaschii (MJ), indicating its role in catalysis.
171 tuted-nucleotides by FtsZ from Methanococcus jannaschii (Mj-FtsZ) and Bacillus subtilis (Bs-FtsZ).
172  reaction analogous to that of Methanococcus jannaschii MJ0044).
173  previously solved enzyme from Methanococcus jannaschii (MJ0109).
174                       The Methanocaldococcus jannaschii MJ0116 gene was cloned and heterologously exp
175 the corresponding protein from Methanococcus jannaschii, MJ0158.
176 t-stable DmrX analog from Methanocaldococcus jannaschii (MJ0208).
177                The protein product of the M. jannaschii MJ0400 gene catalyzes the transaldolase react
178 ve been proposed: one based on Methanococcus jannaschii MJ0577 (1MJH) that binds ATP, and the other b
179 ersion of PRPP to RuBP were identified in M. jannaschii (Mj0601) and Methanosarcina acetivorans (Ma28
180     The protein product of the Methanococcus jannaschii MJ0768 gene has been expressed in Escherichia
181 ed a prototypical ABC NBD, the Methanococcus jannaschii MJ0796, using spectroscopic techniques.
182  by Bacillus subtilis YqeV and Methanococcus jannaschii Mj0867, and we predict that RimO is unique am
183                                Methanococcus jannaschii MJ0936 is a hypothetical protein of unknown f
184 e corresponding gene from Methanocaldococcus jannaschii (mj1022) and characterized the purified recom
185 d that the protein was the product of the M. jannaschii MJ1025 gene.
186                            The Methanococcus jannaschii MJ109 gene product, the sequence of which is
187     The protein product of the Methanococcus jannaschii MJ1256 gene has been expressed in Escherichia
188 oding the DapL homolog in Methanocaldococcus jannaschii (MJ1391) was cloned and expressed in Escheric
189  jannaschii prolyl-tRNA synthetase or the M. jannaschii MJ1477 protein provides the "missing" CysRS a
190         Using four of the Methanocaldococcus jannaschii (Mja) histones, we have examined activation o
191                           Methanocaldococcus jannaschii (Mja) Ptr2, a homologue of the Lrp/AsnC famil
192  conjugate [pre-tRNA(Tyr)-Methanocaldococcus jannaschii (Mja) RPR] to investigate the functional role
193 the C-terminal stirrup of Methanocaldococcus jannaschii (Mja) TBP do not completely abrogate basal tr
194 as that from the archaeon Methanocaldococcus jannaschii (Mja), to catalyze precursor tRNA (ptRNA) pro
195 rom the archaeal organism Methanocaldococcus jannaschii (MjAgo) possesses two modes of action: the ca
196  enzyme from the archaeon Methanocaldococcus jannaschii (MjCobY) in complex with GTP is reported.
197 domain-containing channel from Methanococcus jannaschii, MjK2, by testing its general functional beha
198 the hyperthermophilic archaeon Methanococcus jannaschii (MjMAT) is a prototype of the newly discovere
199 (+) exchanger, NhaP1 from Methanocaldococcus jannaschii (MjNhaP1), a close homologue of the medically
200                           Here,Methanococcus jannaschii MR-ATPgammaS-DNA structure reveals that the p
201 del based on the structures of Methanococcus jannaschii Mre11 (MjMre11) bound to longer DNA molecules
202           The archaeal NCX_Mj (Methanococcus jannaschii NCX) system was used to resolve the backbone
203 change function of an NCX from Methanococcus jannaschii (NCX_Mj) and report its 1.9 angstrom crystal
204             We then tested a hypothetical M. jannaschii O-phosphoseryl-tRNA(Sec) kinase and demonstra
205 of this transformation in Methanocaldococcus jannaschii occurs by the reaction of 4-hydroxybenzoic ac
206 otted protein MJ0366 from Methanocaldococcus jannaschii on the operation of the ClpXP protease from E
207 el complexes derived from Methanocaldococcus jannaschii or Escherichia coli show the channel in its c
208  TAG, together with orthogonal Methanococcus jannaschii or Escherichia coli tRNA/synthetase pairs hav
209                                Methanococcus jannaschii partially retains the superoperon, but lacks
210 f a multidomain protein, as in Methanococcus jannaschii peptidyl-prolyl cis/trans isomerase FKBP26.
211 otein translation apparatus of Methanococcus jannaschii possesses the unusual enzyme prolyl-cysteinyl
212 m5 enzyme of the archaeon Methanocaldococcus jannaschii (previously MJ0883) as an example, we have cr
213 anococcus maripaludis and Methanocaldococcus jannaschii produce cysteine for protein synthesis using
214 us abyssi proabylysin and Methanocaldococcus jannaschii projannalysin), which are soluble and, with a
215                           Methanocaldococcus jannaschii prolyl-tRNA synthetase (ProRS) was previously
216                      It was reported that M. jannaschii prolyl-tRNA synthetase or the M. jannaschii M
217 se results on the in vivo activity of the M. jannaschii ProRS and on the nature of the enzyme involve
218                                  Although M. jannaschii ProRS catalyzes the synthesis of Cys-tRNA(Pro
219                   The archaeal Methanococcus jannaschii ProRS is a member of the eukaryotic-like grou
220 cent biochemical experiments showing that M. jannaschii ProRS misacylates tRNA(Pro) with cysteine, an
221 pure heterologously expressed recombinant M. jannaschii ProRS misaminoacylates M. jannaschii tRNA(Pro
222 ome respects, recognition of tRNA(Pro) by M. jannaschii ProRS parallels that of human, with a strong
223 at resolutions between 2.6 and 3.2 A: apo M. jannaschii ProRS, and M. thermautotrophicus ProRS in apo
224         Studies with human and Methanococcus jannaschii ProRS, which lack a post-transfer editing dom
225 ovide evidence of divergent adaptation by M. jannaschii ProRS; recognition of the tRNA acceptor end i
226 tion NMR study of a model ABC, Methanococcus jannaschii protein MJ1267, reveals that ADP-Mg binding a
227 rted the structure of the Methanocaldococcus jannaschii PSTK (MjPSTK) complexed with AMPPNP.
228 A(Sec) to investigate how Methanocaldococcus jannaschii PSTK distinguishes tRNA(Sec) from tRNA(Ser).
229 mical characterization of Methanocaldococcus jannaschii PSTK, including kinetics of Sep-tRNA(Sec) for
230 ontrast, the effector domain of Ptr1, the M. jannaschii Ptr2 paralogue, yields only very weak activat
231                           Methanocaldococcus jannaschii Ptr2, a member of the Lrp/AsnC family of bact
232 rP, is the product of the Methanocaldococcus jannaschii purP gene (MJ0136), which is a signature gene
233 riosus PurP is structurally homologous to M. jannaschii PurP.
234 gel patterns for Homo sapiens, Methanococcus jannaschii, Pyro coccus furiosus, Shewanella oneidensis,
235 sis of coenzyme F(420) in Methanocaldococcus jannaschii requires generation of 2-phospho-L-lactate, w
236 philes Thermotoga maritima and Methanococcus jannaschii resulted in fivefold higher T. maritima cell
237 rystal structure of the SecY channel from M. jannaschii revealed a plug domain that appears to seal t
238 loped a fluorescently labeled recombinant M. jannaschii RNAP system to probe the archaeal transcripti
239  By studying the archaeal Methanocaldococcus jannaschii RPR's cis cleavage of precursor tRNA(Gln) (pr
240 vir and its analogs inhibit human homolog M. jannaschii S2P cleavage of an artificial protein substra
241  solved X-ray structure of the Methanococcus jannaschii SecY complex, is a matter of contention.
242 d affinity for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate was di
243 s of equivalent plug deletions in SecY of M. jannaschii show that, although the overall structures ar
244 jR31K mutant of PurO from Methanocaldococcus jannaschii showed 76% decreased activity and the MjE102Q
245 us strains from Axial and Methanocaldococcus jannaschii showed similar Monod growth kinetics when gro
246 antiporter NCX_Mj protein from Methanococcus jannaschii shows an outward-facing conformation suggesti
247 ve solved the structure of the Methanococcus jannaschii Spt4/5 complex by X-ray crystallography, and
248     A second dual-guide box C/D sRNA from M. jannaschii, sR6, also exhibited RNA remodeling during te
249 rarchical assembly of the Methanocaldococcus jannaschii sR8 box C/D sRNP is a temperature-dependent p
250                              Surprisingly, M.jannaschii SRP RNA bound to human SRP54M quantitatively
251 r ability to bind to human and Methanococcus jannaschii SRP RNA were determined in vitro.
252 e mechanism of Cys-tRNA(Cys) formation in M. jannaschii still remains to be discovered.
253 hich is different from that of Methanococcus jannaschii, strongly supports an active role in the cata
254 ncy screening was used, 43 of the 44 known M.jannaschii structural ncRNAs were again identified, whil
255 ns, Methanopyrus kandleri, and Methanococcus jannaschii, suggesting a conservation of its function ac
256 phosphate pyrophosphatase from Methanococcus jannaschii that shows a preference for purine base analo
257 protein from the archaeon Methanocaldococcus jannaschii that was copurified with prolyl-tRNA syntheta
258 ebacterium Methanocaldococcus jannaschii (M. jannaschii), the proteasomal regulatory particle (RP), a
259            In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteas
260 ide of 645 amino acids, as for Methanococcus jannaschii, the Sulfolobus solfataricus SSB protein (Sso
261 yclodeaminase is present in the genome of M. jannaschii, these results indicate that proline biosynth
262 ial genomes ranged from 8% for Methanococcus jannaschii to 37% for Mycoplasma pneumoniae.
263 ome-wide occupancy of the Methanocaldococcus jannaschii transcription machinery and its transcriptome
264  CAU and CAC, by an engineered orthogonal M. jannaschii tRNA with an AUG anticodon: tRNA(Opt) We susp
265  the identity elements of Methanocaldococcus jannaschii tRNA(Cys) in the aminoacylation reaction for
266 is unable to aminoacylate purified mature M. jannaschii tRNA(Cys) with cysteine in contrast to facile
267 ow here that the unmodified transcript of M. jannaschii tRNA(Pro) is indeed mis-acylated with cystein
268 nant M. jannaschii ProRS misaminoacylates M. jannaschii tRNA(Pro) with cysteine.
269                            For Methanococcus jannaschii tRNA(Pro), accuracy is difficult because the
270           We introduced a Methanocaldococcus jannaschii tRNA:aminoacyl-tRNA synthetase pair into the
271 uctures of two substrate-bound Methanococcus jannaschii tyrosyl aminoacyl-tRNA synthetases that charg
272 and the genetic code, only the Methanococcus jannaschii tyrosyl tRNA synthetase and tRNA have been us
273                            The Methanococcus jannaschii tyrosyl-transfer-RNA synthetase-tRNA(CUA) (Mj
274 essor tRNA derived from a Methanocaldococcus jannaschii tyrosyl-tRNA (MjtRNATyrCUA) are expressed und
275 ply it to the design of mutant Methanococcus jannaschii tyrosyl-tRNA synthetase (M.jann-TyrRS).
276 r, and a gene encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expresse
277 We synthesized 1 and evolved a Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA(CUA) pair to gen
278 ) that is a substrate for Methanocaldococcus jannaschii TyrRS.
279 hyperthermophilic euryarchaeon Methanococcus jannaschii uses coenzyme M (2-mercaptoethanesulfonic aci
280 te that the Thi4 ortholog from Methanococcus jannaschii uses exogenous sulfide and is catalytic.
281              The archaeon Methanocaldococcus jannaschii uses three different 2-oxoacid elongation pat
282                         MVP, a Methanococcus jannaschii voltage-gated potassium channel, was cloned a
283  presented here, aIF2beta from Methanococcus jannaschii was expressed in Escherichia coli, purified,
284 IMP cyclohydrolase activity in Methanococcus jannaschii was purified and sequenced: its genetic locus
285  Although Methanocaldococcus (Methanococcus) jannaschii was the first archaeon to have its genome seq
286 from the hyperthermophile Methanocaldococcus jannaschii, we describe a functional dissection of this
287 r Typhimurium and the archaeon Methanococcus jannaschii were purified and shown to retain structure.
288 ridium difficile, and Mj2 from Methanococcus jannaschii) were overproduced in Escherichia coli.
289 lyl-tRNA synthetase (ProRS) of Methanococcus jannaschii, which activates both proline and cysteine, t
290 ohydrolase (GCH) III from Methanocaldococcus jannaschii, which catalyzes the conversion of GTP to 2-a
291 -1.9 A) structures of PSP from Methanococcus jannaschii, which define the open state prior to substra
292 siae, and archaebacterium Methanocaldococcus jannaschii, which encodes a protein with no homology to
293 nal tyrosine pair derived from Methanococcus jannaschii, which has been used to selectively incorpora
294 ydrolase III protein from Methanocaldococcus jannaschii, which has no amino acid sequence homology to
295 of the archaeal CorA from Methanocaldococcus jannaschii, which is a unique complete structure of a Co
296 ified cell extracts of M. thermophila or Mc. jannaschii with 7,8-didemethyl-8-hydroxy-5-deazariboflav
297 cell extracts of both M. thermophila and Mc. jannaschii with [hydroxy-(18)O, carboxyl-(18)O(2)]lactat
298 erthermophilic methanogen Methanocaldococcus jannaschii with bound substrate dihydroxyacetone phospha
299 on of cell extracts of M. thermophila or Mc. jannaschii with either LPPG or LPPA and Fo generated F(4
300 eductase (RNR) using the recently evolved M. jannaschii Y-tRNA synthetase/tRNA pair.

 
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