ライフサイエンスコーパス: dsRBM

1 along with an NMR study of the binding of a dsRBM derived from the Drosophila protein Staufen, indic

2 Both dsRBMs have an intrinsic ability to dimerize (dsRBM2) or

3 y with one dsRBM, while others can bind both dsRBMs of PKR.

4 intact PKR N terminus (p20) containing both dsRBMs.

5 peptide required to bind dsRNA contains both dsRBMs, as determined by mobility-shift and filter-bindi

6 hypothesis that simultaneous binding of both dsRBMs of PKR occurs on kinase activating RNA ligands.

7 tion, has two copies of the highly conserved dsRBM motif.

8 that the unique binding preferences of each dsRBM differentially contribute to their pleiotropic fun

9 a highly conserved RNA-binding site on each dsRBM and suggests a novel mode of protein-RNA recogniti

10 ed questions regarding the role(s) that each dsRBM plays in ADAR2 function.

11 lso contain a U1-like zinc finger and either dsRBM or Pumilio motifs.

12 udy, we site-specifically modified the first dsRBM of PKR's RBD at two different amino acid positions

13 fication of binding sites for the individual dsRBMs on various RNA ligands including a viral activati

14 the double-stranded (ds) RNA binding motif (dsRBM) of the vaccinia virus E3 protein.

15 e or more double-stranded RNA binding motif (dsRBM) that play important roles in small RNA biogenesis

16 ed of two copies of the dsRNA binding motif (dsRBM).

17 ed of two copies of the dsRNA binding motif (dsRBM).

18 esses three copies of a dsRNA-binding motif (dsRBM).

19 wo tandem copies of the dsRNA-binding motif (dsRBM).

20 wo tandem copies of the dsRNA-binding motif (dsRBM).

21 ains two double stranded RNA-binding motifs (dsRBMs) and interacts with highly structured RNAs as wel

22 sing two tandem linked dsRNA-binding motifs (dsRBMs) both with an alpha-beta-beta-beta-alpha fold.

23 interact with the two dsRNA-binding motifs (dsRBMs) in its N terminus.

24 p74 contains two dsRNA-binding motifs (dsRBMs) that are essential for preferential binding to d

25 o tandem double-stranded RNA-binding motifs (dsRBMs) that are not only important for efficient editin

26 ization signal and two dsRNA-binding motifs (dsRBMs), and are identical at their N termini.

27 R2's two double-stranded RNA-binding motifs (dsRBMs), and the correct placement of the nucleoside ana

28 inding sites for PKR's dsRNA binding motifs (dsRBMs).

29 lar plants, four distinct clades of multiple dsRBM DRBs are always present with the exception of Bras

30 phylogenetic approach, we show that multiple dsRBM DRBs are systematically composed of two different

31 matically composed of two different types of dsRBMs evolving under different constraints and likely f

32 dicate that some RNAs interact only with one dsRBM, while others can bind both dsRBMs of PKR.

33 ns and cytological activities of the two PKR dsRBMs (dsRBM1 and dsRBM2) and the cooperation between t

34 nosine (BndG) blocked interaction with PKR's dsRBMs and inhibited activation of PKR by the siRNA.

35 e named DRB7) whose members possess a single dsRBM that shows concerted evolution with the most C-ter

36 concerted evolution with the most C-terminal dsRBM domain of the Dicer-like 4 (DCL4) proteins.

37 This supports the notion that dsRBM-containing proteins can bind to RNAs with secondar

38 e Drosophila protein Staufen, indicates that dsRBMs can bind stem-loop RNAs in distinct ways.

39 substrate-dependent manner, indicating that dsRBMs recognize distinct structural determinants in eac

40 The dsRBM is a conserved protein motif found in many protein

41 The dsRBM is an alpha-beta-beta-beta-alpha structure present

42 To assess the functional selectivity of the dsRBM motifs in ADAR1, we constructed and characterized

43 onstrating the functional selectivity of the dsRBM motifs.

44 er staufen) and in many other members of the dsRBM protein family.

45 accinia virus E3 map to the same face of the dsRBM structure and are thus likely to compose part of t

46 demonstrate that NF110b associates with the dsRBM-containing transcriptional co-activator, RNA helic

47 The dsRBMs of ADAR2 are interchangeable for subnuclear targe

48 RNA-dependent interaction is mediated by the dsRBMs of the two proteins.

49 y, we site-specifically modified each of the dsRBMs of PKR's dsRBD with the hydroxyl radical generato

50 Here, we demonstrate that the dsRBMs of ADAR2 differ in both their ability to modulate

51 This study shows that the dsRBMs of PKR possess distinct properties and that some,

52 characterized chimeric proteins in which the dsRBMs of ADAR1 were substituted with those of PKR.

53 n suggests this approach could be applied to dsRBMs found in other proteins.

54 e biochemical interactions between these two dsRBM containing proteins.

55 al substrates, substitution of the first two dsRBMs of ADAR1 with those from PKR dramatically reduced

56 These six residues are conserved in the two dsRBMs for which structural information is available (Es

57 Chimeric deaminases possessing only the two dsRBMs from PKR were incapable of editing either glutama

58 is highly flexible, which may enable the two dsRBMs to wrap around the RNA duplex for cooperative and

59 r amino acid residues (NVKQ) between the two dsRBMs.

60 t of cooperativity in the binding of the two dsRBMs.