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1 T. thermophilus EF-Ts functions only as a homodimer.
2 T. thermophilus HB8 RNA polymerase (RNAP) recognizes mid
3 T. thermophilus Kt-23 has two further non-Watson-Crick b
4 T. thermophilus NDH-1 contains at most nine putative iro
5 T. thermophilus showed no such transition within the tem
8 s of three primary proteins from E. coli and T. thermophilus 30S subunits that bind early in the asse
10 rather similar dnaX sequences in E. coli and T. thermophilus lead to very different mechanisms of exp
12 urvey the folding stabilities of E. coli and T. thermophilus proteomes at various temperatures and pr
13 ults of the binding of RecA from E. coli and T. thermophilus show adaptation to pressure and temperat
14 of labeled membranes of P. denitrificans and T. thermophilus established photoaffinity labeling of th
15 on the crystal structures of human DIPP1 and T. thermophilus Ndx1, were generated using homology mode
17 bility of key translation components between T. thermophilus and E. coli, and the functional conserva
18 did not inhibit transcription initiation by T. thermophilus RNAP in vitro or shorten the lifetimes o
19 Methylation of 30S ribosomal subunits by T. thermophilus KsgA is more efficient at low concentrat
20 ia coli catabolite activator protein (CAP)], T. thermophilus RNAP sigma(A) holoenzyme, a class II TAP
21 e lifetimes of promoter complexes containing T. thermophilus RNAP, in contrast to the conclusion in t
24 wider range of pressure and temperature for T. thermophilus compared to E. coli RecA, suggesting a c
27 eratures, the heat capacity of unfolding for T. thermophilus RNase H is lower, resulting in a smaller
28 nus of its bacterial homolog (subunit C from T. thermophilus) stabilized the yeast subunit d mutant 3
29 elenomethione-substituted apical domain from T. thermophilus was determined to a resolution of 1.78 A
32 y crystal structures of PRODH and P5CDH from T. thermophilus, a model was built for a proposed PRODH-
33 m18-negative tRNA with recombinant trmH from T. thermophilus abolished its IFN-alpha inducing potenti
35 se that the primary role of TtAgo is to help T. thermophilus disentangle the catenated circular chrom
38 e identified a novel transcription factor in T. thermophilus and T. aquaticus that shares a high degr
42 hat the transcriptional regulation of mer in T. thermophilus is both similar to, and different from,
44 ate and spectrum of spontaneous mutations in T. thermophilus resembled those of the thermoacidophilic
47 mulated over 20 single-base substitutions in T. thermophilus 16S and 23S rRNA, in the decoding site a
50 s of new chimeric proteins reveals that like T. thermophilus RNase H, the folding core of C. tepidum
51 ibute to an overall reduction in activity of T. thermophilus ribonuclease H compared to its mesophili
52 stimulate the intrinsic cleavage activity of T. thermophilus RNA polymerase, and increase the k(app)
53 cterizing the intrinsic cleavage activity of T. thermophilus RNA polymerase, we have identified, clon
54 imentally observed conformational changes of T. thermophilus leucyl-tRNA synthetase upon substrate bi
55 e PutA PRODH domain, the FAD conformation of T. thermophilus PRODH is remarkably different and likely
62 e, employing the latest crystal structure of T. thermophilus complex I, we have used microsecond-scal
63 clear evidence that the pilus structures of T. thermophilus are not essential for natural transforma
64 Here we report five crystal structures of T. thermophilus enzyme in complex with NADH or quinone-l
67 gion and comparisons with similar studies on T. thermophilus RNase H, identify new residues involved
69 domain) of ba(3)-type cytochrome c oxidase (T. thermophilus) (pI = 6.0) exhibit optimal voltammetric
73 ion complex provide compelling evidence that T. thermophilus RNA polymerase can bind to DNA containin
76 ant shows no growth defects, indicating that T. thermophilus PrmA, like its E. coli homolog, is dispe
78 a broad phylogenetic range, suggesting that T. thermophilus may be an ideal model system for the stu
79 the UV-sensitive phenotype, suggesting that T. thermophilus RuvB protein has a function similar to t
87 within the dimer interface that disrupt the T. thermophilus EF-Ts dimer but not the tertiary structu
89 e is inserted after position 80 to mimic the T. thermophilus protein reproduce the differences in con
90 teins, relative binding free energies of the T. thermophilus 30S proteins to the 16S RNA were studied
91 deled on the known crystal structures of the T. thermophilus acyl-CoA synthetase with remarkably high
93 te that mutations increasing activity of the T. thermophilus enzyme at mesophilic temperatures do so
98 es, we have developed an atomic model of the T. thermophilus ribosome using a homology modeling appro
99 In accordance, we find that growth of the T. thermophilus strain with an inactivated C1942 methylt
100 mparing the membrane-embedded regions of the T. thermophilus V/A-ATPase and eukaryotic V-ATPase from
102 the III-B system the result implies that the T. thermophilus III-B system must elicit a more efficien
103 These results strongly suggest that the T. thermophilus NDH-1 is similar to other NDH-1 enzyme c
104 With the advantage of thermostability, the T. thermophilus NDH-1 provides a great model system to i
105 By mapping significant DNA motifs to the T. thermophilus HB8 genome, we identify potentially regu
106 of the antibiotic telithromycin bound to the T. thermophilus ribosome reveals a lactone ring with a c
108 rganisms, and the contacts observed with the T. thermophilus ribosome are consistent with biochemical
110 riophage PH75, which infects the thermophile T. thermophilus, assembles in vivo at 70 degrees C and i
112 show that binding of a Thermus thermophilus (T. thermophilus) Csm (TthCsm) to a nascent transcript in
114 e-stranded DNA endonuclease activity of this T. thermophilus domain is activated not by magnesium but
115 e X-ray crystal structure revealed that this T. thermophilus glucose binding protein (ttGBP) is struc
117 thermore, the interdomain angle of wild-type T. thermophilus goes from 81 degrees to 118 degrees wher