ライフサイエンスコーパス: histone-like

1 that the sigma factors also possess a linker histone-like activity in the formation of a prokaryotic

2 packaged with protein VII, a virally encoded histone-like core protein that is suggested to protect i

3 aging protein in yeast, like its prokaryotic histone-like counterpart, HU protein.

4 HU, a nonspecific histone-like DNA binding protein, participates in a numb

5 This study identified HP119 as a putative histone-like DNA-binding protein and showed that it play

6 anded-DNA-binding 12RNP2 precursor (HP0827); histone-like DNA-binding protein HU (HP0835); ribosomal

7 the pandemic clone of V. parahaemolyticus, a histone-like DNA-binding protein, HU-alpha, has a C-term

8 onstrates that the evolutionarily conserved, histone-like domain is sufficient and necessary to suppo

9 lterin proteins TRF1 or TRF2, also possess a histone-like domain which is involved in protein-protein

10 specific genes; rather, MeCP2 functions as a histone-like factor whose phosphorylation may facilitate

11 Lsr2 is a M. tuberculosis protein with histone-like features, including the ability to regulate

12 nts, including two novel human proteins with histone-like folds and sequence relationships to yeast S

13 including the ubiquitous HU proteins, serve histone-like functions in prokaryotes.

14 identity with the consensus sequence of the histone-like HB protein of Bacillus species.

15 The histone-like HU (heat unstable) protein plays a key role

16 pret new experimental data for the bacterial histone-like HU protein and two eukaryotic high-mobility

17 These data reveal histone-like modification cassettes - or "histone mimics

18 uence homologies and propose that an ancient histone-like motif in two CBF subunits controls the form

19 response sigma factor (sigmas), and H-NS, a histone-like nucleoid protein and global transcription r

20 The histone-like nucleoid structuring (H-NS) protein plays a

21 tion from these promoters is silenced by the histone-like nucleoid structuring (H-NS) protein.

22 ors that participate in this process are the histone-like nucleoid structuring protein (H-NS) and the

23 The histone-like nucleoid structuring protein (H-NS) has bee

24 The histone-like nucleoid structuring protein (H-NS) is a DN

25 The histone-like nucleoid structuring protein (H-NS) is a nu

26 Histone-like nucleoid structuring protein (H-NS) is repr

27 We found that the histone-like nucleoid structuring protein (H-NS) selecti

28 hat are believed to facilitate DNA bridging: histone-like nucleoid structuring protein (H-NS), ParB,

29 erve as binding sites for the gene repressor histone-like nucleoid structuring protein (H-NS), we mea

30 The histone-like nucleoid structuring protein H-NS and DNA s

31 also found to be structurally similar to the histone-like nucleoid structuring protein H-NS, indicati

32 ent a mutant of Escherichia coli lacking the histone-like nucleoid structuring protein H-NS.

33 e silencer EAT6 was capable of replacing the histone-like nucleoid structuring protein nucleation fun

34 ncer AT8 is a nucleation site for recruiting histone-like nucleoid structuring protein to form a cis-

35 E is repressed by the global regulator H-NS (histone-like nucleoid structuring protein), but can be a

36 The histone-like nucleoid structuring protein, H-NS, is a pr

37 Members of the histone-like nucleoid-structuring (H-NS) family of prote

38 We recently found that histone-like nucleoid-structuring protein (H-NS) binds t

39 r, foreign DNA appears to be silenced by the histone-like nucleoid-structuring protein (H-NS) in seve

40 Histone-like nucleoid-structuring protein (H-NS) is an a

41 Global colocalization of the histone-like nucleoid-structuring protein (H-NS) with Rh

42 scription of virulence genes silenced by the histone-like nucleoid-structuring protein (H-NS).

43 ssect this mechanism for a model system: the Histone-like Nucleoid-Structuring protein (H-NS).

44 rm into rows [as on binding of the bacterial histone-like nucleoid-structuring protein (H-NS)], large

45 sr2 appears to be a unique protein with both histone-like properties and protective features that may

46 The histone like protein HctA is central to RB:EB differenti

47 In contrast, the histone-like protein (H-NS) and the stationary-phase sig

48 in vitro transcription assay, we showed that histone-like protein (HLP), a homologue of Escherichia c

49 The histone-like protein (HlpA) is highly conserved among st

50 In addition to its role in the nucleoid, the histone-like protein (HlpA) of Streptococcus pyogenes is

51 y includes integration host factor (IHF) and histone-like protein (HU); both are present in the extra

52 tase (SP-STP) and their endogenous substrate histone-like protein (SP-HLP).

53 Consequently, we propose this bifunctional histone-like protein as a candidate that could structura

54 PRM2 is a histone-like protein essential to spermatogenesis and wa

55 The effects of HU, the histone-like protein from Escherichia coli, on the equil

56 nomical approach for gene delivery using the histone-like protein from the hyperthermostable eubacter

57 ption from this promoter is repressed by the histone-like protein H-NS and requires OmpR-P for induct

58 s a stable complex with the Escherichia coli histone-like protein H-NS and transfer RNAs (tRNAs).

59 richia coli and to determine the role of the histone-like protein H-NS in this environmental regulati

60 teomic analysis, we found that the bacterial histone-like protein H-NS interacts with Arn, implying a

61 The histone-like protein H-NS is a major component of the ba

62 Here, we report that the histone-like protein H-NS is an aerobic repressor of cyd

63 ly acquired genes, which are silenced by the histone-like protein H-NS.

64 rotein Csp15, and increased synthesis of the histone-like protein H-NS.

65 by cell extract requires the presence of the histone-like protein H-NS.

66 pBA transcription even in the absence of the histone-like protein H-NS.

67 One of the known targets of histone-like protein H1 is flhDC, the master operon whic

68 2A, respectively, and to the archaebacterial histone-like protein HMf-2.

69 (E) and O(I), specifically interact with the histone-like protein HU and close the loop in supercoile

70 tion of plectoneme-free regions, whereas the histone-like protein HU and SMC (structural maintenance

71 omarkers that allow such discrimination: the histone-like protein HU form B, the 10 kDa chaperonin Cp

72 The histone-like protein HU from Escherichia coli is involve

73 erved much slower dissociation kinetics of a histone-like protein HU from the whole chromosome during

74 The histone-like protein HU is involved in compaction of the

75 phosphate, a DNA-bending protein such as the histone-like protein HU or integration host factor (IHF)

76 gal operators (OE and OI) and binding of the histone-like protein HU to a specific locus (hbs) about

77 he gal promoters also requires the bacterial histone-like protein HU which acts as a co-factor.

78 a coli requires Gal repressor (GalR) and the histone-like protein HU.

79 may contribute to such processes include the histone-like protein HU.

80 vely supercoiled DNA and the presence of the histone-like protein HU.

81 disclose the in vivo organization of a viral histone-like protein in bacteria.

82 ith high identity to zebrafish H1M, a linker histone-like protein involved in primordial germ cell sp

83 odies to streptolysin O, indicating that the histone-like protein is released by group A streptococci

84 s identified a direct repressor of bfrB, the histone-like protein Lsr2.

85 The gene, termed tcbC, encoded a histone-like protein of 14.5 kDa.

86 ophage 29 protein p6 has been described as a histone-like protein that compacts the viral genome by f

87 Integration host factor (IHF) is a bacterial histone-like protein whose primary biological role is to

88 with FliF (the MS ring protein) and H-NS (a histone-like protein).

89 d, the expression of the gene coding for the histone-like protein, hns, was significantly derepressed

90 Here we present data showing that the histone-like protein, HU, has a role in the molecular pa

91 s flanking the promoters, (2) the binding of histone-like protein, HU, to a site between the GalR-bin

92 two distal operators, and the binding of the histone-like protein, HU, to an architecturally critical

93 Using an altered bacterial histone-like protein, HUalpha, we show that reorganizati

94 activator, and is repressed by YmoA, a small histone-like protein.

95 By contrast, 'histone-like' protein (i.e. Fis, IHF and H-NS) -binding

96 Histone-like proteins (such as HU, H-NS, and Fis) partic

97 iption is required in cells deficient in the histone-like proteins Fis or IHF.

98 s components of Escherichia coli pre-RC, two histone-like proteins HU and IHF (integration host facto

99 while non-specific binding of IHF and other histone-like proteins serves to structure the nucleoid.

100 protein has some features characteristic of histone-like proteins, and we showed that purified HP119

101 The chlamydial histone-like proteins, Hc1 and Hc2, function as global r

102 unlike other structurally related bacterial histone-like proteins, IHF has evolved a sequence-depend

103 ain DNA-binding proteins, such as histone or histone-like proteins, to modulate topology of chromosom

104 e specific nucleoprotein complexes involving histone-like proteins, which repress promoter activity w

105 ed two independent acquisitions of bacterial histone-like proteins.

106 paternal genome and replaces sperm-specific histone-like proteins.

107 tein of influenza A H3N2 subtype possesses a histone-like sequence (histone mimic) that is used by th

108 ic transcription factor (TF) composed of two histone-like subunits (NF-YB and NF-YC) and a sequence-s

109 results strongly suggest the existence of a histone-like surface on TFIID.

110 This is the first demonstration that a non-histone-like TAF is required for continuous, high level

111 responsible for expression of cTAF(II)31, a histone-like TAF(II) residing in both the transcription

112 Unexpectedly, we find that the histone-like TAF(II)s have distinct roles in expression

113 subunits shared by TFIID and SAGA are three histone-like TAF(II)s, which have been proposed to form

114 It was shown previously that three histone-like TAFs are broadly required for transcription

115 for TAFs in transcription, we find that the histone-like TAFs are generally required for in vivo tra

116 s, indicating its loss of function, like the histone-like TAFs, causes degradation of the constituent

117 ilizing interactions of TAFs, especially the histone-like TAFs, in TFIID.

118 ressed by overexpression of any of the other histone-like TAFs.

119 e of the gene encoding TAF25p, that this non-histone-like TBP-associated factor, which is shared betw