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1 B. stearothermophilus also encodes an RNA-binding protei
3 lutamate transporters from B. caldotenax and B. stearothermophilus and localize exposed and accessibl
5 52 and G2553 of 23S rRNA in both E. coli and B. stearothermophilus ribosomal RNA and incorporated int
6 ysis of tyrosine activation by the human and B. stearothermophilus enzymes indicates that despite dif
7 Kinetic analyses of recombinant human and B. stearothermophilus tyrosyl-tRNA synthetases expressed
9 s among the yeast R65Q, equine, porcine, and B. stearothermophilus PGK structures occur in the relati
12 helical content of the linker fragment from B. stearothermophilus is 68% at high pH and 1 degree C.
13 se with the NAD(+)-dependent DNA ligase from B. stearothermophilus, two independent functional domain
14 ited forms of phosphofructokinase (PFK) from B. stearothermophilus have led to a structural model for
16 ormation of the tyrosyl-adenylate complex in B. stearothermophilus are conserved across all of the or
18 tion state for the activation of tyrosine in B. stearothermophilus tyrosyl-tRNA synthetase (Cys-35, H
20 -tRNA synthetase aminoacylates human but not B. stearothermophilus tRNATyr, and vice versa, supportin
22 -specific CPS were not affected by growth of B. stearothermophilus at temperatures near the minimal g
23 ical regardless of the growth temperature of B. stearothermophilus between 42 degrees C and 63 degree
25 ylogenetic analysis of spoIIA suggested that B. stearothermophilus is close to B. subtilis and B. lic
28 n these two domains is different than in the B. stearothermophilus iPGM structure determined previous
29 S4 and 5' domain RNA suggest that it is the B. stearothermophilus S4, not the rRNA, that is activate
30 s corresponding to the linker regions of the B. stearothermophilus and the E. coli protein were synth
31 gth dependence of the helical content of the B. stearothermophilus peptide demonstrates that side-cha
32 the isolated N and C-terminal domains of the B. stearothermophilus protein suggest that the linker fo
35 a poly(G) polymerase; and we transformed the B. stearothermophilus CCA-adding enzyme into a poly(C,A)
36 charge distributions, and packing within the B. stearothermophilus TRAP crystal form does not generat
37 t allow direct comparison to a thermophilic (B. stearothermophilus) ortholog, Ec-DHFR and Bs-DHFR, re
40 high resolution crystal structures of yeast, B. stearothermophilus, T. brucei and T. maritima PGK, an
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