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1                               Where present, Methanocaldococcus genes were the predominant mcrA/mrtA
2 that there was generally sufficient H(2) for Methanocaldococcus growth at Axial but not at Endeavour.
3 we demonstrate that NifB from the methanogen Methanocaldococcus infernus is a radical SAM enzyme able
4 bacter vinelandii with NifB from the archaea Methanocaldococcus infernus or Methanothermobacter therm
5 rystallographic structure of an Ogg2 member, Methanocaldococcus janischii Ogg, in complex with a DNA
6                              The enzyme from Methanocaldococcus jannachii is designated MptB (MJ0837
7                       In the archaebacterium Methanocaldococcus jannaschii (M. jannaschii), the prote
8 d a binary Ago-guide complex of the archaeal Methanocaldococcus jannaschii (Mj) Ago.
9                           The interaction of Methanocaldococcus jannaschii (Mj) Nop56/58 with the met
10  discovery of an isopentenyl kinase (IPK) in Methanocaldococcus jannaschii (MJ) suggests a new variat
11 ffective with a heat-stable DmrX analog from Methanocaldococcus jannaschii (MJ0208).
12   We also cloned the corresponding gene from Methanocaldococcus jannaschii (mj1022) and characterized
13        The gene encoding the DapL homolog in Methanocaldococcus jannaschii (MJ1391) was cloned and ex
14                            Using four of the Methanocaldococcus jannaschii (Mja) histones, we have ex
15                                              Methanocaldococcus jannaschii (Mja) Ptr2, a homologue of
16                    A recent cryo-EM study of Methanocaldococcus jannaschii (Mja) RNase P produced a m
17 ed substrate-enzyme conjugate [pre-tRNA(Tyr)-Methanocaldococcus jannaschii (Mja) RPR] to investigate
18 e substitutions in the C-terminal stirrup of Methanocaldococcus jannaschii (Mja) TBP do not completel
19 f these RPRs, such as that from the archaeon Methanocaldococcus jannaschii (Mja), to catalyze precurs
20 rt that Argonaute from the archaeal organism Methanocaldococcus jannaschii (MjAgo) possesses two mode
21 hanism of base activation by the PRTase from Methanocaldococcus jannaschii (MjCobT), we solved crysta
22 ltransferase (CobY) enzyme from the archaeon Methanocaldococcus jannaschii (MjCobY) in complex with G
23 ctroneutral Na(+)/H(+) exchanger, NhaP1 from Methanocaldococcus jannaschii (MjNhaP1), a close homolog
24        Using the Trm5 enzyme of the archaeon Methanocaldococcus jannaschii (previously MJ0883) as an
25 o proteins in Escherichia coli using evolved Methanocaldococcus jannaschii aminoacyl-tRNA synthetase(
26 ed by borrelidin, whereas ThrRS enzymes from Methanocaldococcus jannaschii and Archaeoglobus fulgidus
27 s, to several orthogonal aaRSes derived from Methanocaldococcus jannaschii and Escherichia coli tyros
28         Full length homologues were found in Methanocaldococcus jannaschii and Methanothermobacter th
29 y recombinant ProRS enzymes from the archaea Methanocaldococcus jannaschii and Methanothermobacter th
30                     The methanogenic archaea Methanocaldococcus jannaschii and Methanothermobacter th
31 r created two RPAs that mimicked the RPAs in Methanocaldococcus jannaschii and Methanothermobacter th
32 , Mj0400 and Mj1249, have been identified in Methanocaldococcus jannaschii as the enzymes involved in
33     In the case of the methanogenic archaeon Methanocaldococcus jannaschii as well as most methanogen
34 ntron (both linear and circular forms) using Methanocaldococcus jannaschii box C/D RNP core proteins.
35 ically active box C/D sRNP from the archaeon Methanocaldococcus jannaschii by single-particle electro
36 inity of PaNhaP and the related MjNhaP1 from Methanocaldococcus jannaschii can be attributed to an ad
37 crystal structures of FAICAR synthetase from Methanocaldococcus jannaschii complexed with various lig
38  found that the prototypical NBD MJ0796 from Methanocaldococcus jannaschii dimerizes in response to A
39 s 99% similar to that of non-nitrogen fixing Methanocaldococcus jannaschii DSM 2661.
40 d purified the corresponding fragment of the Methanocaldococcus jannaschii Elp3 protein.
41 the hyperthermophilic, methanogenic archaeon Methanocaldococcus jannaschii encodes a CobY protein (Mj
42    Here, we report that the MJ0438 gene from Methanocaldococcus jannaschii encodes a novel S-adenosyl
43               The hyperthermophilic archaeon Methanocaldococcus jannaschii encodes a potent transcrip
44  similar to that of the C-terminal domain of Methanocaldococcus jannaschii endonuclease.
45                      Here we report that the Methanocaldococcus jannaschii enzyme derived from the MJ
46 pCysS (Cys(64), Cys(67), and Cys(272) in the Methanocaldococcus jannaschii enzyme) are essential for
47 1003 and MJ1271 proteins from the methanogen Methanocaldococcus jannaschii formed the first homoaconi
48                                              Methanocaldococcus jannaschii gene MJ1179 encodes a prot
49 d an uncharacterized archaeal protein in the Methanocaldococcus jannaschii genome, MJ0887, which coul
50                     The riboflavin kinase in Methanocaldococcus jannaschii has been identified as the
51 mation of lactaldehyde and hydroxyacetone in Methanocaldococcus jannaschii have been established.
52 rystal structure of an engineered variant of Methanocaldococcus jannaschii Hsp16.5 wherein a 14 amino
53 ickel site distinct from that of zinc-loaded Methanocaldococcus jannaschii HypB as well as subtle cha
54   Here we present the structure of KsgA from Methanocaldococcus jannaschii in complex with several li
55 of the Nep1 homolog from the archaebacterium Methanocaldococcus jannaschii in its free form (2.2 A re
56 es that contrasted with the related organism Methanocaldococcus jannaschii included the absence of in
57 ification of the corresponding activity from Methanocaldococcus jannaschii indicated that tRNA(Cys) b
58                                              Methanocaldococcus jannaschii is a hypertheromphilic, st
59                              The enzyme from Methanocaldococcus jannaschii is designated MptA to indi
60 encoded by the MJ0619 gene in the methanogen Methanocaldococcus jannaschii is likely this missing met
61  report that the enzyme encoded by Mj0883 of Methanocaldococcus jannaschii is the archaeal counterpar
62 nases associated with isoprene biosynthesis, Methanocaldococcus jannaschii isopentenyl phosphate kina
63 ccharomyces cerevisiae, Escherichia coli and Methanocaldococcus jannaschii It presents the following
64                     The crystal structure of Methanocaldococcus jannaschii L7Ae has been determined t
65                                          The Methanocaldococcus jannaschii MJ0116 gene was cloned and
66 py, the first step of this transformation in Methanocaldococcus jannaschii occurs by the reaction of
67 s of the trefoil-knotted protein MJ0366 from Methanocaldococcus jannaschii on the operation of the Cl
68 ribosome-SecY channel complexes derived from Methanocaldococcus jannaschii or Escherichia coli show t
69                Methanococcus maripaludis and Methanocaldococcus jannaschii produce cysteine for prote
70  of these (Pyrococcus abyssi proabylysin and Methanocaldococcus jannaschii projannalysin), which are
71                                              Methanocaldococcus jannaschii prolyl-tRNA synthetase (Pr
72     Earlier we reported the structure of the Methanocaldococcus jannaschii PSTK (MjPSTK) complexed wi
73 cus maripaludis tRNA(Sec) to investigate how Methanocaldococcus jannaschii PSTK distinguishes tRNA(Se
74 y presents a biochemical characterization of Methanocaldococcus jannaschii PSTK, including kinetics o
75                                              Methanocaldococcus jannaschii Ptr2, a member of the Lrp/
76  we designate as PurP, is the product of the Methanocaldococcus jannaschii purP gene (MJ0136), which
77 ps in the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii requires generation of 2-p
78                     By studying the archaeal Methanocaldococcus jannaschii RPR's cis cleavage of prec
79               The MjR31K mutant of PurO from Methanocaldococcus jannaschii showed 76% decreased activ
80 wo Methanocaldococcus strains from Axial and Methanocaldococcus jannaschii showed similar Monod growt
81 resent high-resolution cryo-EM structures of Methanocaldococcus jannaschii sHSP (mjHSP16.5) in apo an
82                 Hierarchical assembly of the Methanocaldococcus jannaschii sR8 box C/D sRNP is a temp
83 f a non-synthetase protein from the archaeon Methanocaldococcus jannaschii that was copurified with p
84 aracterized the genome-wide occupancy of the Methanocaldococcus jannaschii transcription machinery an
85       We determined the identity elements of Methanocaldococcus jannaschii tRNA(Cys) in the aminoacyl
86                              We introduced a Methanocaldococcus jannaschii tRNA:aminoacyl-tRNA synthe
87 ding an amber suppressor tRNA derived from a Methanocaldococcus jannaschii tyrosyl-tRNA (MjtRNATyrCUA
88 r tRNA (itRNA(Ty2) ) that is a substrate for Methanocaldococcus jannaschii TyrRS.
89                                 The archaeon Methanocaldococcus jannaschii uses three different 2-oxo
90  G1PDH from the hyperthermophilic methanogen Methanocaldococcus jannaschii with bound substrate dihyd
91 aracterize here the MJ1541 gene product from Methanocaldococcus jannaschii, an enzyme that was annota
92 om three archaea: Methanococcus maripaludis, Methanocaldococcus jannaschii, and Sulfolobus solfataric
93 d biochemically, in the sequenced genomes of Methanocaldococcus jannaschii, Bacillus cereus ATCC 1098
94 foldin (gammaPFD) in the deep-sea methanogen Methanocaldococcus jannaschii, is integral to understand
95 of the ORFs had their highest Blastp hits in Methanocaldococcus jannaschii, lateral gene transfer or
96                      However, the genomes of Methanocaldococcus jannaschii, Methanothermobacter therm
97 ing this protein have not been identified in Methanocaldococcus jannaschii, Methanothermobacter therm
98                               In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric
99                     In some archaea, such as Methanocaldococcus jannaschii, these lipids are further
100 nit RNA polymerase from the hyperthermophile Methanocaldococcus jannaschii, we describe a functional
101            GTP cyclohydrolase (GCH) III from Methanocaldococcus jannaschii, which catalyzes the conve
102 accharomyces cerevisiae, and archaebacterium Methanocaldococcus jannaschii, which encodes a protein w
103 ed for a GTP cyclohydrolase III protein from Methanocaldococcus jannaschii, which has no amino acid s
104 solution structure of the archaeal CorA from Methanocaldococcus jannaschii, which is a unique complet
105 its simplicity, we studied the Trx system of Methanocaldococcus jannaschii--a deeply rooted hyperther
106 like proteins from Clostridium difficile and Methanocaldococcus jannaschii.
107 ed in the archaeal pathway leading to DHQ in Methanocaldococcus jannaschii.
108 nd the 12-subunit RNA polymerase (RNAP) from Methanocaldococcus jannaschii.
109 th-like activity in extracts of the archaeon Methanocaldococcus jannaschii.
110 ical examination of DHNA from the methanogen Methanocaldococcus jannaschii.
111 cture of Dim1 from the thermophilic archaeon Methanocaldococcus jannaschii.
112 hod to search for promoters in the genome of Methanocaldococcus jannaschii.
113 itrogen-fixing hyperthermophilic methanogen, Methanocaldococcus jannaschii.
114 e core domain of an S2P metalloprotease from Methanocaldococcus jannaschii.
115 ugar for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii.
116  and that of the homologous E/F complex from Methanocaldococcus jannaschii.
117 ate has been isolated and characterized from Methanocaldococcus jannaschii.
118 ion reaction, and it was recently shown that Methanocaldococcus (Methanococcus) jannaschii and other
119                                     Although Methanocaldococcus (Methanococcus) jannaschii was the fi
120                                          Two Methanocaldococcus strains from Axial and Methanocaldoco
121 ucidate the structure of the archaellum from Methanocaldococcus villosus at 3.08 angstrom resolution.
122 n factor IIB of Methanococcus jannaschii and Methanocaldococcus vulcanius, revealing a novel modified

 
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