ライフサイエンスコーパス: modification enzyme

1 ain (TRD) of EcoKI, a type I restriction and modification enzyme.

2 when a target site is recognised by the core modification enzyme.

3 g both as a transcription factor and an rRNA-modification enzyme.

4 to the complete bifunctional restriction and modification enzyme.

5 from that of other ATP-dependent restriction-modification enzymes.

6 A binding site of type I DNA restriction and modification enzymes.

7 tent inhibitor of type I DNA restriction and modification enzymes.

8 -binding domains associated with DNA and RNA modification enzymes.

9 on changes with charge alterations caused by modification enzymes.

10 rbohydrate in conjunction with several sugar-modification enzymes.

11 chaperones, foldases, and post-translational modification enzymes.

12 g three novel targets for type I restriction/modification enzymes.

13 DNA-binding groove of Type I DNA restriction/modification enzymes.

14 ing multiple hematopoietic TFs and chromatin-modification enzymes.

15 by regulation of cell envelope synthesis and modification enzymes.

16 sitive to the relative composition of the HS modification enzymes.

17 ctivities of other protein posttranslational modification enzymes.

18 rough a dynamic interplay with other histone-modification enzymes.

19 ng enzymatic corepressors, including histone modification enzymes.

20 gulation mediated by G9a and other chromatin modification enzymes.

21 hed the Ae. aegypti genome for candidate DNA modification enzymes.

22 omain that is found in several tRNA and rRNA modification enzymes.

23 f target recognition by Type ISP restriction-modification enzymes.

24 ription, and in the action of DNA repair and modification enzymes.

25 s has a family of phase-variable restriction-modification enzymes.

26 resulfated heparin and revealed the critical modification enzymes.

27 Using the EcoR124I restriction-modification enzyme, a 3'-5' double-strand DNA (dsDNA) t

28 itude lower than that of other purified tRNA modification enzymes, a Kmapp (DMAPP) = 632 nM, and a kc

29 may serve as a functional paradigm for other modification enzymes acting late in 30S biogenesis.

30 Here we test the hypothesis that RNA modification enzymes also act as RNA chaperones.

31 te, and the ksgA gene, which encodes an rRNA modification enzyme and is partly cotranscribed with pdx

32 that connects RNA polymerase I with ribosome modification enzymes and remodels the translational prog

33 transcription factors and this family of RNA modification enzymes and that h-mtTFB may perform dual f

34 quires the sequential recruitment of histone modification enzymes and the general transcription facto

35 e complexity of substrate recognition by RNA modification enzymes and the potential for direct involv

36 e in vivo interactions between the chromatin modification enzymes and their actual nucleosomal substr

37 target sequence and which is present on the modification enzyme, and a region on each DNA cleavage s

38 to an F-box protein and recognition by early modification enzymes, and the effect of binding is dimin

39 nes had homology to putative DNA restriction-modification enzymes, and two had homology to putative m

40 d auxiliary metabolic functions, restriction modification enzymes, and virion structural proteins, al

41 We discuss the likelihood that other RNA modification enzymes are also RNA chaperones.

42 Type I restriction-modification enzymes are differentiated from type II and

43 very similar, although the overall levels of modification enzymes are higher.

44 Lipid A modification enzymes are reporters for lipopolysaccharid

45 The S subunits of type I DNA restriction/modification enzymes are responsible for recognising the

46 The prokaryotic Type ISP restriction-modification enzymes are single-chain proteins comprisin

47 the key roles of tRNA modifications and tRNA modification enzymes as checkpoints for tRNA integrity a

48 ying disruptions in genes encoding chromatin modification enzymes, but are not significantly expresse

49 d linker (i) makes pentapeptide available to modification enzymes by separation from the helical rece

50 nctional data indicate that specific histone modification enzymes can be key to longevity in Caenorha

51 was unaffected by the presence of the methyl-modification enzymes, CheB and CheR, or the coupling pro

52 imilarity between the two companion receptor modification enzymes, CheB and CheR, suggests an evoluti

53 The Type I restriction-modification enzymes comprise three protein subunits; Hs

54 of both type I and type III restriction and modification enzymes contains motifs characteristic of D

55 The type I restriction and modification enzymes do not possess obvious DNA-binding

56 subunit of the bacterial Type I restriction-modification enzyme EcoKI during restriction alleviation

57 tivity of a helicase, the Type I restriction modification enzyme EcoR124I.

58 Likewise some tRNA modification enzymes either require iron-sulfur clusters

59 LlaGI is a single polypeptide restriction-modification enzyme encoded on the naturally-occurring p

60 f Mycoplasma pulmonis encode restriction and modification enzymes exhibiting a high degree of sequenc

61 s unclear is how specific members of histone modification enzyme families, such as histone methyltran

62 equires the sequential production of the new modification enzyme followed by the restriction activity

63 We screened mutants of several RNA modification enzymes for an effect on RpoS expression an

64 alA1 and HalA2 are processed by the purified modification enzymes HalM1 and HalM2 in an in vitro reco

65 A long-term goal in the field of restriction-modification enzymes has been to generate restriction en

66 indicating that most, if not all, of the end modification enzymes have been identified.

67 nnections between these proteins and histone modification enzymes have emerged as a common theme, imp

68 Additional gene products, such as chromatin modification enzymes, have unanticipated effects on pre-

69 lar RNAs are chemically modified by many RNA modification enzymes; however, often the functions of mo

70 nce that exposure to an inhibitor of histone modification enzymes implicated in epigenetic control of

71 nthase 1 (Pus1p) is an unusual site-specific modification enzyme in that it can modify a number of po

72 titative rate analysis for posttranslational modification enzymes in complex milieus for native subst

73 for the role of haploinsufficency of histone-modification enzymes in multiple-congenital-anomaly synd

74 These data implicate histone modification enzymes in suppressing DC-derived IL-12, wh

75 lmost all of the genes coding for the t+rRNA modification enzymes in the mesophilic moderate halophil

76 than for the minimal system of receptor and modification enzymes in vitro.

77 Because the modification enzyme is not present in prokaryotes, no na

78 Targeting of protein modification enzymes is a key biochemical step to achiev

79 sion of two translocating Type I Restriction-Modification enzymes is not fully understood.

80 s facilitate enzymatic activities of histone modification enzymes is unclear.

81 eave DNA, the single polypeptide restriction-modification enzyme LlaGI must communicate between a pai

82 domain of the single polypeptide restriction-modification enzyme LlaGI reveals amino acid motifs char

83 strate that the related Type ISP Restriction-Modification enzymes LlaGI and LlaBIII can cooperate to

84 Heterologous expression of lipid A modification enzymes may enable the development of new v

85 We suggest that histone modification enzymes may re-establish the histone code o

86 subcellular distribution of Mod5p-I, a tRNA modification enzyme, member of the sorting isozyme famil

87 ygfZ reduced the activities of the Fe/S tRNA modification enzyme MiaB and certain other Fe/S enzymes,

88 Although not required for growth, the modification enzymes modulate virulence of some gram-neg

89 e of a new sub-classification of Restriction-Modification enzymes, named Type I SP (for Single Polype

90 s of cell stress, the type I restriction and modification enzymes of bacteria show reduced, but not z

91 The type I DNA restriction and modification enzymes of prokaryotes are multimeric enzym

92 NA element that regulates downstream encoded modification enzymes of queuosine biosynthesis.

93 trast, is a 1105-aa Type IIC restriction-and-modification enzyme, one of a family of Thermus homologs

94 rategy by which many poorly understood lipid modification enzymes operate.

95 be reported that encodes a posttranslational modification enzyme, palmitoyltransferase.

96 r (TF) binding motifs, and several chromatin modification enzymes preferentially interact with these

97 em couples three different posttranslational modification enzymes, prohormone convertases (PCs), carb

98 Type I DNA restriction/modification enzymes protect the bacterial cell from vir

99 downstream of the gene encoding its putative modification enzyme, RamC.

100 some biogenesis requires the presence of the modification enzyme rather than its RNA-modifying cataly

101 of synthetic interactions with several tRNA modification enzymes, resulting in temperature-sensitive

102 mutant strains and those lacking diphthamide modification enzymes showed increased -1 frameshifting.

103 A global survey of tRNA modification enzymes shows that the functional constrain

104 ein-protein interactions, post-translational modifications, enzyme-substrate relationships and diseas

105 tein-protein interactions, posttranslational modifications, enzyme/substrate relationships, disease a

106 hen a mutation in TRM6, which encodes a tRNA modification enzyme subunit, was combined with the delet

107 Acps also include modification enzymes such as proteases and their inhibit

108 eshold, in opposite direction to that of the modification enzymes suggesting that the latter reduce S

109 lusters by genes encoding post-translational modification enzymes that carry out lantibiotic-type deh

110 dentify a new subgroup of Type I Restriction-Modification enzymes that modify cytosine in one DNA str

111 f the hexa-acylated lipid A species, several modification enzymes then function to produce the major

112 binding surfaces to assemble select histone modification enzymes, thereby specifying the pattern of

113 The tRNA modification enzymes ThiI (in bacteria and archaea) and

114 ng the interaction site for the adaptational-modification enzymes to the carboxyl terminus of induced

115 tein, denoting the strict specificity of the modification enzymes toward the substrate protein.

116 base-pairs, almost identical to that of the modification enzyme which makes up the core of EcoKI.

117 gene cassettes encode several aminoglycoside modification enzymes, which correlate with most of the a

118 A type I restriction-modification enzyme will bind to an unmethylated target

119 othesized that HpyIII, a type II restriction/modification enzyme with sequence homology to MboI, medi

120 to encode a 49-amino-acid peptide (YydF), a modification enzyme (YydG), a membrane-embedded protease