ライフサイエンスコーパス: elongation factor G

1 by RRF (ribosome recycling factor) and EF-G (elongation factor G).

2 compensated by mutations in the translation elongation factor G.

3 n, encompassing the first 293 amino acids of elongation factor G.

4 mbled by ribosome recycling factor (RRF) and elongation factor G.

5 ve dissected early folding events of nascent elongation factor G, a multi-domain protein that require

6 This implies that elongation factor G actively pushes both the decoding si

7 ent translational GTPase factors, along with elongation factor G and BPI-inducible protein A.

8 on change in Efl1 equivalent to changes that elongation factor G and eEF2 undergo during translocatio

9 he two release factors is as good as between elongation factor G and elongation factor Tu-guanosine-5

10 Subsequent binding of elongation factor G and GTP hydrolysis results in a cloc

11 osomes at a site that coincides with that of elongation factor G and has a GTPase activity that is se

12 The translation factors, elongation factor G and ribosome recycling factor, are k

13 st our method on the experimental cryo-EM of elongation factor G and show that the model obtained is

14 ational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4).

15 ver, the antibiotic has negligible effect on elongation factor G catalyzed translocation of tRNA and

16 Elongation factor-G-catalyzed translocation of mRNA and

17 e single-dimer ribosomal particles supported elongation factor G dependent GTP hydrolysis and protein

18 scribe a new sensitive method for monitoring elongation factor G-dependent translocation of the mRNA

19 of this base-pair in peptide bond formation, elongation factor G-dependent translocation, and peptide

20 inked ribosomes were specifically blocked in elongation factor G-dependent translocation.

21 iostrepton, which inhibits the activities of elongation factor G (EF-G) and EF-Tu by binding to the r

22 Ribosome recycling factor (RRF), elongation factor G (EF-G) and GTP split 70S ribosomes i

23 enger RNA (mRNA), in a reaction catalyzed by elongation factor G (EF-G) and guanosine triphosphate (G

24 The antibiotic fusidic acid (FA) targets elongation factor G (EF-G) and inhibits ribosomal peptid

25 It inhibits protein synthesis by binding to elongation factor G (EF-G) and preventing its release fr

26 Elongation factor G (EF-G) and ribosome recycling factor

27 ion (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of

28 led into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling fa

29 During protein synthesis, elongation factor G (EF-G) binds to the ribosome and pro

30 After peptide-bond formation, elongation factor G (EF-G) binds to the ribosome, trigge

31 nt crystal structures of G proteins, such as elongation factor G (EF-G) bound to the ribosome, as wel

32 bits bacterial protein synthesis by blocking elongation factor G (EF-G) catalyzed translocation of me

33 The guanosine triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent move

34 The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation o

35 ibosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termin

36 complex through the ribosome is promoted by elongation factor G (EF-G) during the translation cycle.

37 f mRNA-tRNAs through the ribosome, bacterial elongation factor G (EF-G) hydrolyzes energy-rich guanos

38 ction of ribosome recycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphat

39 ough the ribosome is catalyzed by the GTPase elongation factor G (EF-G) in bacteria.

40 ersally conserved ribosome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation

41 coding region, resulting from the binding of elongation factor G (EF-G) in various forms.

42 Initiation factor 2 (IF2) and elongation factor G (EF-G) induce similar changes in rib

43 Elongation factor G (EF-G) is a guanosine triphosphatase

44 Elongation factor G (EF-G) is a universally conserved tr

45 Binding of elongation factor G (EF-G) shifts this equilibrium towar

46 the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational rib

47 Elongation factor G (EF-G) was identified as one possibl

48 In contrast, the activity of elongation factor G (EF-G) was strongly impaired in alph

49 ociation of elongation factor Tu (EF-Tu) and elongation factor G (EF-G) with the ribosome during prot

50 ation step of prokaryotic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (

51 In elongation factor G (EF-G), a highly conserved protein c

52 tion of the ribosome-recycling factor (RRF), elongation factor G (EF-G), and GTP to prepare the ribos

53 bosome-recycling factor (RRF), together with elongation factor G (EF-G), disassembles this posttermin

54 Tet(M) protein, which displays homology to elongation factor G (EF-G), interacts with the protein b

55 ct with an elongated form of the translation elongation factor G (EF-G), leading to the suggestion th

56 Mediated by elongation factor G (EF-G), ribosome translocation along

57 , ribosome-recycling factor (RRF) and GTPase elongation factor G (EF-G), synergistically split 100S r

58 These proteins bind to elongation factor G (EF-G), the target of FA, and rescue

59 rotated state is not a proper substrate for elongation factor G (EF-G), thus inhibiting translocatio

60 elivers aminoacyl tRNAs to the ribosome, and elongation factor G (EF-G), which catalyzes translocatio

61 The elongation factor G (EF-G)-catalyzed translocation of mR

62 We observed significantly slower elongation factor G (EF-G)-catalyzed translocation throu

63 Cryo-EM reconstructions of certain elongation factor G (EF-G)-containing complexes have led

64 anied by large interdomain rearrangements of elongation factor G (EF-G).

65 zed by the guanosine triphosphatase (GTPase) elongation factor G (EF-G).

66 drolysis on elongation factor Tu (EF-Tu) and elongation factor G (EF-G).

67 nslation by interfering with the function of elongation factor G (EF-G).

68 n of the ribosome-recycling factor (RRF) and elongation factor G (EF-G).

69 nslocation through the ribosome catalyzed by elongation factor G (EF-G).

70 f elongation and translocation by the GTPase elongation factor G (EF-G).

71 RRF(mt)) and a recycling-specific homolog of elongation factor G (EF-G2(mt)).

72 This reaction is catalyzed by elongation factor-G (EF-G) and is associated with riboso

73 Ribosome recycling factor (RRF) and elongation factor-G (EF-G) are jointly essential for rec

74 The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-term

75 e to FA by rescuing the translocation factor Elongation Factor-G (EF-G) from FA-stalled ribosome comp

76 presence of the antibiotic thiostrepton and elongation factor-G (EF-G) rigorously localized the bind

77 ogenic bacteria Staphylococcus aureus, locks elongation factor-G (EF-G) to the ribosome after GTP hyd

78 ly of proteins that bind to the drug target (Elongation factor G [EF-G]) and promote dissociation of

79 R) of an orthologue of bacterial translation elongation factor G (EFG).

80 ional ribosome complexes and to compete with elongation factor G for interaction with pretranslocatio

81 of the small subunit head domain within the elongation factor G (GDP)-bound ribosome complex.

82 domains could facilitate the association of elongation factor-G into lipid rafts in living bacteria,

83 As a homolog of elongation factor G, it contains three domains (III-V) p

84 o observe aa-tRNA accommodation coupled with elongation factor G-mediated translocation.

85 Mitochondria possess two elongation factor Gs: one with translocation activity (E

86 We can position either elongation factor G or elongation factor Tu complexed wi

87 The overproduction of elongation factor G or initiation factor 3 did not have

88 m the A to the P-site upon GTP hydrolysis by elongation factor G, shifting approximately 8 A toward t

89 ur findings reveal that the bacterial GTPase elongation factor G specifically engages spontaneously a

90 domain (L11-NTD) may variously interact with elongation factor G, the antibiotic thiostrepton, and rR

91 In the absence of elongation factor G, the entire pretranslocation ribosom

92 recycling factor (RRF) is used together with elongation factor G to recycle the 30S and 50S ribosomal

93 mal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a com

94 d also shows time-dependent enhancement when elongation factor G with GTP is added to 70S ribosomes.