ライフサイエンスコーパス: lambda repressor

1 domain with a dimerization domain (as in the lambda repressor).

2 ed to replace the dimerization domain of the lambda repressor.

3 ntegrase linked to the DNA-binding domain of lambda repressor.

4 actually reached by the Oct-1 POU domain and lambda repressor.

5 to lambda cI phages as the wild-type, intact lambda repressor.

6 ll-atom folding simulations of ubiquitin and lambda-repressor.

7 utants of an 80-residue-long fragment of the lambda-repressor.

8 We concentrate on chymotrypsin inhibitor and lambda-repressor.

9 bent when bound by Cro than in the case with lambda-repressor.

10 Ala-29 of Cro and the backbone of Gly-46 of lambda-repressor.

11 was constructed consisting of a fragment of lambda repressor, a decahistidine tag, an intervening TE

12 Bacteriophage lambda repressor activates transcription from P(RM) by c

13 Degradation in vivo of lambda repressor amino-terminal domain variants bearing

14 Variants of lambda repressor and cytochrome b562 translated from mes

15 igns for the B1 domain of protein G, for the lambda repressor and for sperm whale myoglobin are prese

16 The bacteriophage lambda repressor and its relatives bind cooperatively to

17 For lambda repressor and YbeL, the SsrA-H6 tag was added aft

18 erize DNA loops induced by the lac, gal, and lambda repressors and (ii) understand the mechanistic ro

19 igher degree of cooperativity than seen with lambda repressor, and previous evidence has suggested th

20 article) and T. G. Oas and co-workers on the lambda-repressor, and helps to clarify the differences o

21 lexes of catabolite-activator protein (CAP), lambda-repressor, and their corresponding uncomplexed pr

22 velop a monomeric C-terminal fragment of the lambda repressor as a novel fluorescent probe that speci

23 By using the DNA-binding domain of lambda repressor as a reporter for invasin self-interact

24 interaction, using the DNA binding domain of lambda repressor as a reporter.

25 The discrimination of Cro and lambda-repressor between their different operators is mo

26 igands DAPI, netropsin, lexitropsin, and the lambda repressor binding domain.

27 oping of single DNA molecules containing the lambda repressor binding sites separated by 2317 bp (the

28 egration in vitro into target DNA containing lambda repressor binding sites.

29 milar switch regulates the virus life cycle; lambda repressor binds to an operator site and blocks tr

30 Our data show that unlike bacteriophage lambda, repressor bound at O(L) of bacteriophage 933W ha

31 The three-dimensional structure of the lambda repressor C-terminal domain (CTD) has been determ

32 e present the x-ray crystal structure of the lambda repressor C-terminal domain determined by multiwa

33 O(L) (separated by 2.3 kb), mediated by the lambda repressor CI (accession number P03034), play key

34 ltaneously measured the concentration of the lambda repressor CI and the number of messenger RNAs (mR

35 Tolerance to the lambda repressor cI sequence p1-102 or its immunodominan

36 inding interaction between the bacteriophage lambda-repressor CI and its target DNA using total inter

37 tly, it was proposed that DNA looping by the lambda repressor (CI protein) strengthens repression of

38 The lambda repressor (CI) maintains the quiescent (lysogenic

39 The lambda repressor (CI) protein-induced DNA loop maintains

40 Lambda repressor cleaves itself at the peptide bond betw

41 in of the entropy difference between CAP and lambda-repressor complexation arises more from the addit

42 have designed a hyper-cleavable fragment of lambda repressor containing the hinge and C-terminal dom

43 ambda repressor-ToxR chimeric proteins and a lambda repressor-controlled reporter system (OR1 PR-lacZ

44 ere, we have determined the structure of the lambda repressor CTD in three new crystal forms, under a

45 minal half of E3 in the yeast two-hybrid and lambda repressor dimerization assays.

46 t a model for the cooperative binding of two lambda repressor dimers at adjacent operator sites.

47 peptides that support oligomerization of the lambda repressor DNA-binding domain in Escherichia coli

48 no acid alphabets were fused in-frame to the lambda repressor DNA-binding domain to provide an in viv

49 y to the helix-turn-helix (HTH) motif of the lambda repressor DNA-binding domain.

50 a murine IgG1 tolerogen, both expressing the lambda repressor epitope 12-26.

51 We apply the method to lambda repressor fragment 6-85 and fyn-SH3.

52 as been applied to three different proteins (lambda repressor fragment 6-85, chymotrypsin inhibitor 2

53 The extent of self-cleavage of a lambda repressor fragment in the presence of RecA, ADP-A

54 dicted that a very fast folding protein like lambda repressor fragment lambda(6-85) D14A could have a

55 utant Tyr22Trp/Glu33Tyr/Gly46Ala/Gly48Ala of lambda repressor fragment lambda(6-85) was previously as

56 e, we study pressure-drop refolding of three lambda-repressor fragment (lambda(6-85)) mutants computa

57 n lambda*YA, the Y22W/Q33Y/G46,48A mutant of lambda-repressor fragment 6-85, from 3 mus to 5 ms after

58 upport the molecular time scale inferred for lambda-repressor from near-downhill folding experiments,

59 self-interacting proteins that re-constitute lambda repressor function.

60 prising the N-terminal DNA binding domain of lambda repressor fused to a fragment of a foreign protei

61 e formation of full-length PKR dimers in the lambda repressor fusion and two-hybrid systems.

62 demonstrated in vivo using the bacteriophage lambda repressor fusion assay.

63 Deletion analysis with the lambda repressor fusion system identified a previously u

64 Using a lambda repressor fusion technique, 10 Bcep781-encoded pr

65 random DNA fragments cloned into a series of lambda repressor fusion vectors were subjected to select

66 stability by approximately 30-50 kcal/mol in lambda repressor, GCN4 coiled coil, and cytochrome c but

67 A tryptophan-containing variant of monomeric lambda repressor has been made, and its folding kinetics

68 ried residues Asp 14 and Ser 77 in monomeric lambda repressor has been removed by mutation of these r

69 of residues 6-85 of the N-terminal domain of lambda repressor have been determined by fitting the thr

70 impact on a field, as the lac repressor and lambda repressor have had in Molecular Biology in bacter

71 mp refolding experiments on the helix bundle lambda-repressor have shown evidence of a <3 mus burst p

72 ether with the flexible hinge region of the (lambda) repressor (Hex-(lambda)VP2).

73 The structure provides a unique snapshot of lambda repressor in a conformation that sheds light on h

74 tively dimerize the amino-terminal domain of lambda repressor in Escherichia coli.

75 nt study, the folding mechanism of monomeric lambda repressor is described using the diffusion-collis

76 While lambda-repressor is known to tolerate any hydrophobic mu

77 lambda-Repressor is stable and well folded, while MarA a

78 -cap motifs of the 5-helix protein monomeric lambda repressor (lambda(6-85)) and have measured the ra

79 e to the DNA-binding domain of bacteriophage lambda repressor leads to the formation of functional, d

80 st for the specificity of dimer formation by lambda repressor-leucine zipper fusions.

81 and Ser-28 in Cro, and Gln-44 and Ser-45 in lambda-repressor, make very similar interactions with th

82 ed two retroviral constructs encoding the cI lambda repressor (MBAE-1-102 and MBAE-1-102-IgG) for gen

83 y populates the denatured state of monomeric lambda repressor (MetO-lambdaLS) under nondenaturing con

84 Whereas the overall fold of the 186 and lambda repressor monomers is remarkably similar, the way

85 tected refolding of a genetically engineered lambda repressor mutant from its pressure-denatured stat

86 Here we show that a lambda-repressor mutant is nonetheless capable of refold

87 ous work shows that the energy landscapes of lambda repressor mutants support all standard folding me

88 -4-loop-helix-5 portions) of variants of the lambda repressor operator binding domain, using an ECEPP

89 sus, a non-specific DNA control based on the lambda repressor operator OR1 and two model sequence tar

90 r 'crossing' have been established using the lambda repressor-operator system: the specific complex c

91 Previously characterized lambda repressor/operator complexes occupy an intermedia

92 f presenting exogenously added ovalbumin and lambda repressor peptides.

93 ure the oligomerization of the bacteriophage lambda repressor protein at micromolar concentrations.

94 to obtain the free energy of binding of the lambda repressor protein to the OR1 operator DNA sequenc

95 g mutant forms of the NH2-terminal domain of lambda repressor protein to the secreted protein inverta

96 The mediator of these processes is the lambda repressor protein, CI, and its interactions with

97 is maintained by a highly regulated level of lambda repressor protein, CI, which represses lytic func

98 e temporal evolution of the concentration of lambda repressor protein.

99 dimensional structures of the lambda-Cro and lambda-repressor proteins in complex with DNA has made i

100 , monomeric form of the N-terminal domain of lambda repressor, refolds with a lifetime of approximate

101 gh resolution crystal structure of the phage lambda repressor reveals the basis for repressor dimer f

102 students and I worked out the regulation of lambda repressor synthesis for the establishment and mai

103 influence the maintenance of lysogeny in the lambda repressor system; it can encode sensitivity to th

104 olved topic, especially for proteins such as lambda-repressor that fold on the microsecond timescale.

105 In lambda-repressor the helices are 34 A apart and are esse

106 DNA by CI in solution, where in contrast to lambda repressor, the looped species were exceptionally

107 , because of the small size of ubiquitin and lambda-repressor, these states are short-lived.

108 very stable lambdaHA is the fastest-folding lambda repressor to date (k(f)(-1) approximately k(obs)(

109 Binding of the N-terminal domain of the lambda repressor to DNA is coupled to dimerization.

110 ed bacteriophage lambda, in which binding of lambda repressor to either lambdaO(R)1 or lambdaO(R)2 re

111 especially 2 and 4) are used by both Cro and lambda-repressor to differentiate the operator sites as

112 Previous experiments using lambda repressor-ToxR chimeric proteins and a lambda rep

113 temperature, with the most hydrophobic one, lambda-repressor, undergoing a reexpansion at the highes

114 o are reported for a small globular protein, lambda repressor, using the "C(m) experiment".

115 he lambda and P22 repressors; we show that a lambda repressor variant bearing the P22 residues at the

116 ies of maltose binding protein and monomeric lambda repressor variants determined by SUPREX agree wel

117 ed cooperative interactions is that of phage lambda repressor, which binds cooperatively to two adjac

118 owth of phage lambda is the self-cleavage of lambda repressor, which is induced by the formation of a