ライフサイエンスコーパス: B. stearothermophilus

1 B. stearothermophilus also encodes an RNA-binding protei

2 r kinases in B. halodurans, B. anthracis and B. stearothermophilus.

3 lutamate transporters from B. caldotenax and B. stearothermophilus and localize exposed and accessibl

4 mperatures of optimum growth for E. coli and B. stearothermophilus (3% versus 17%).

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

8 B. subtilis, B. polymyxa, and B. stearothermophilus shared few AFLP markers with B. an

9 s among the yeast R65Q, equine, porcine, and B. stearothermophilus PGK structures occur in the relati

10 As expected, the TRAP:RNA complex from B. stearothermophilus is significantly more thermostable

11 more flexible in the thermophilic DHFR from B. stearothermophilus.

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

15 , slowly extended by the DNA polymerase from B. stearothermophilus in a template-directed manner.

16 In B. stearothermophilus IF3, these two compact domains are

17 ormation of the tyrosyl-adenylate complex in B. stearothermophilus are conserved across all of the or

18 show a high degree of similarity to those in B. stearothermophilus iPGM.

19 tion state for the activation of tyrosine in B. stearothermophilus tyrosyl-tRNA synthetase (Cys-35, H

20 It was found that (i) intact B. stearothermophilus L11 binds rRNA with K approximatel

21 -tRNA synthetase aminoacylates human but not B. stearothermophilus tRNATyr, and vice versa, supportin

22 lipoyl domain in the presence and absence of B. stearothermophilus E1p were recorded.

23 -specific CPS were not affected by growth of B. stearothermophilus at temperatures near the minimal g

24 ical regardless of the growth temperature of B. stearothermophilus between 42 degrees C and 63 degree

25 Like the B. subtilis protein, B. stearothermophilus TRAP has 11 subunits arranged in a

26 ylogenetic analysis of spoIIA suggested that B. stearothermophilus is close to B. subtilis and B. lic

27 e human tyrosyl-tRNA synthetase than for the B. stearothermophilus enzyme.

28 an tyrosyl-tRNA synthetase than it is in the B. stearothermophilus enzyme.

29 n these two domains is different than in the B. stearothermophilus iPGM structure determined previous

30 S4 and 5' domain RNA suggest that it is the B. stearothermophilus S4, not the rRNA, that is activate

31 s corresponding to the linker regions of the B. stearothermophilus and the E. coli protein were synth

32 gth dependence of the helical content of the B. stearothermophilus peptide demonstrates that side-cha

33 the isolated N and C-terminal domains of the B. stearothermophilus protein suggest that the linker fo

34 In contrast to the B. stearothermophilus enzyme, catalysis of the tyrosine

35 We also transformed the B. stearothermophilus CCA-adding enzyme into a dCdCdA-ad

36 a poly(G) polymerase; and we transformed the B. stearothermophilus CCA-adding enzyme into a poly(C,A)

37 charge distributions, and packing within the B. stearothermophilus TRAP crystal form does not generat

38 t allow direct comparison to a thermophilic (B. stearothermophilus) ortholog, Ec-DHFR and Bs-DHFR, re

39 ly from those seen with the M. tuberculosis, B. stearothermophilus and other enzymes.

40 Analyses of AT interaction with B. stearothermophilus TRAP at 60 degrees C demonstrated

41 high resolution crystal structures of yeast, B. stearothermophilus, T. brucei and T. maritima PGK, an