ライフサイエンスコーパス: snoRNP

1 fied but a homolog for the eukaryotic 15.5kD snoRNP protein has not been described.

2 teins are involved in the formation of H/ACA snoRNP and telomerase complexes, both involved in essent

3 d in a cotranscriptional manner during H/ACA snoRNP assembly, possibly by binding to the nascent H/AC

4 d in the early biogenesis steps of box H/ACA snoRNP assembly.

5 ain is essential for Shq1p function in H/ACA snoRNP biogenesis in vivo, possibly in an Hsp90-independ

6 er, we show that NOP10, a component of H/ACA snoRNP complexes including telomerase is mutated in a la

7 olved in the early biogenesis steps of H/ACA snoRNP complexes, and Shq1p depletion leads to a specifi

8 Each H/ACA snoRNP consist of four conserved proteins, Cbf5 (the Psi

9 he former is associated with all yeast H/ACA snoRNP core proteins, unlike TLC1 RNA, the endogenous RN

10 ortance of the association of hTR with H/ACA snoRNP core proteins, we have attempted to express hTR i

11 he TbMTr1 complex specializes the SLA1 H/ACA snoRNP for efficient processing of multiple modification

12 uman hUTP23 directly interact with the H/ACA snoRNP protein yNhp2/hNHP2, the RNA helicase yRok1/hROK1

13 We show that the presence of the H/ACA snoRNP proteins Cbf5p, Nhp2p and Nop10p, but not Gar1p,

14 eins Spt16p, Tfg1p, and Sub1p and with H/ACA snoRNP proteins.

15 ssociation with three of the four core H/ACA snoRNP proteins.

16 he cellular level of pseudouridine, an H/ACA snoRNP-mediated modification of rRNA and other RNAs that

17 hich is likely to be common to all box H/ACA snoRNP-substrate complexes.

18 ity for Shq1p and a direct link to the H/ACA snoRNP.

19 p is the Psi synthase component of box H/ACA snoRNPs and suggest that the pseudouridylation of rRNA,

20 Nonetheless, functional H/ACA snoRNPs assembled in cytosolic extracts are stable and d

21 abilizes the association of Nhp2p with H/ACA snoRNPs expressed in vivo.

22 Ps or mature Cbf5- and Gar1-containing H/ACA snoRNPs from tgs1Delta cells.

23 g protein Naf1p, which is required for H/ACA snoRNPs stability, associates with RNA polymerase II-ass

24 ng the four conserved core proteins of H/ACA snoRNPs, a kinetoplastid-specific protein designated met

25 associated with two core components of H/ACA snoRNPs, hGar1p and Dyskerin (the human counterpart of y

26 Among the known protein components of H/ACA snoRNPs, the essential nucleolar protein Cbf5p is the mo

27 haracterized NAP57 is specific for box H/ACA snoRNPs, whereas the newly identified NAP65, the rat hom

28 skerin is the catalytic subunit of box H/ACA snoRNPs.

29 y are not strongly associated with box H/ACA snoRNPs.

30 Cbf5p, two core proteins of mature box H/ACA snoRNPs.

31 and required for the stability of box H/ACA snoRNPs.

32 that yeast telomerase is unrelated to H/ACA snoRNPs.

33 f TMG caps, nor was the composition of H/ACA snoRNPs.

34 nd is probably not a common component of all snoRNPs.

35 Although snoRNP composition has been thoroughly characterized, th

36 report of a protein component specific to an snoRNP essential for processing of the large ribosomal s

37 er, RNA degradation, snRNA modification, and snoRNP biogenesis).

38 well-characterized murine model of the anti-snoRNP autoimmune response, for the ability to selective

39 immunogenic/antigenic material for the anti-snoRNP response in scleroderma.

40 s common protein subunits with the H/ACA box snoRNPs.

41 divergent box C'/D' motifs that are bound by snoRNP proteins.

42 -negative mutant of SMN (SMNDeltaN27) causes snoRNPs to accumulate outside of the nucleolus in struct

43 is of small nucleolar RNA-protein complexes (snoRNPs) consists of synthesis of the snoRNA and protein

44 arge population of snoRNA-protein complexes (snoRNPs), which create modified nucleotides and particip

45 small nucleolar ribonucleoprotein complexes (snoRNPs) via the targeting of Nhp2 and Nop58.

46 thesis of the snoRNA and protein components, snoRNP assembly, and localization to the nucleolus.

47 o impairs localization of C/D and H/ACA core snoRNP proteins Nop1p and Gar1p, suggesting a defect(s)

48 d TIP49 make multiple interactions with core snoRNP proteins and biogenesis factors and that these in

49 n sequence to Nop58p, is a bona fide box C+D snoRNP component; all tested box C+D snoRNAs were coprec

50 P complexes, but their exact role in box C/D snoRNP biogenesis is largely uncharacterized.

51 factors are directly involved in U8 box C/D snoRNP biogenesis.

52 ins are restructured during human U3 box C/D snoRNP biogenesis; however, the molecular basis of this

53 ific protein component of functional box C/D snoRNP complexes.

54 Archaeal homologs of the box C/D snoRNP core proteins fibrillarin and Nop56/58 have also

55 and support an asymmetric model for box C/D snoRNP organization.

56 stem to demonstrate that assembly of box C/D snoRNP proteins is the step affected by snoRNA location,

57 ey functional nucleoproteins such as box C/D snoRNP.

58 Our data argue that box C/D snoRNPs are asymmetric, with the C' box contacting Nop56

59 small nucleolar ribonucleoproteins (box C/D snoRNPs in eukaryotes), respectively.

60 associated with mature Nop58-containing C/D snoRNPs or mature Cbf5- and Gar1-containing H/ACA snoRNP

61 lar size and promote localization of box C/D snoRNPs to nucleoli, suggesting a role in rRNA maturatio

62 e protein composition and association of C/D snoRNPs with the small subunit (SSU) processosome were n

63 sing (RNase P), RNA modification (H/ACA, C/D snoRNPs), and translation (ribosomes), especially by emp

64 Box C/D snoRNPs, factors essential for ribosome biogenesis, are

65 The assembly and maturation of box C/D snoRNPs, factors essential for ribosome biogenesis, occu

66 r coupling also occurs in eukaryotic box C/D snoRNPs.

67 t are essential for the formation of box C/D snoRNPs.

68 gesting that this may occur with all box C/D snoRNPs.

69 rk for understanding the assembly of box C/D snoRNPs.

70 propose that each snoRNA forms two different snoRNPs, subtly different in how the proteins are bound

71 In contrast to the eukaryotic snoRNP complex, where the core proteins are distributed

72 nsight into the highly homologous eukaryotic snoRNPs.

73 nts of the U3 snoRNP, representing the first snoRNP components identified by using the two-hybrid met

74 n, and that active splicing is essential for snoRNP assembly.

75 Among the factors required for snoRNP biogenesis in yeast is Shq1p, an essential protei

76 it to act as a molecular adaptor for guiding snoRNP assembly in similar fashion in all archaea and eu

77 However, snoRNP biogenesis in vivo requires multiple factors to c

78 s Nop1p and Gar1p, suggesting a defect(s) in snoRNP assembly or trafficking to the nucleolus.

79 ting that they function at an early stage in snoRNP biogenesis.

80 expression causes a substantial increase in snoRNPs associated with 60S-90S preribosomal RNP complex

81 In contrast, splicing-independent snoRNP assembly can occur in vitro on snoRNAs that posse

82 ding yeast) for maturation and assembly into snoRNPs prior to accumulation in their primary functiona

83 e we present a characterization of mammalian snoRNPs.

84 A mature snoRNP has been reconstituted in vitro and is composed o

85 e bridging biogenesis factors, to the mature snoRNP.

86 U14 processing snoRNPs and several modifying snoRNPs examined.

87 The possibility that modifying snoRNPs might affect ribosome structure in other ways is

88 vestigate this process, we have analyzed non-snoRNP factors associated with the nucleoplasmic human U

89 he core box C/D proteins as well as many non-snoRNP factors linked to snoRNP assembly (TIP48, TIP49,

90 Moreover, the Nopp140-snoRNP interaction appears to be conserved in yeast, bec

91 anism for preventing premature activation of snoRNP catalytic activity.

92 orated in vivo by the exclusive depletion of snoRNP proteins from nucleoli in cells transfected with

93 nding of the timing and ordered hierarchy of snoRNP action in pre-40S maturation and reveal a novel m

94 ion and reveal a novel mode of regulation of snoRNP function by an RNA helicase in human cells.

95 umor suppressor p53 can act as a sentinel of snoRNP perturbation, the activation of which mediates th

96 cleroderma fibroblasts, suggests a source of snoRNP to initiate and maintain these autoantibody respo

97 ghetti is necessary for the stabilization of snoRNP core proteins and target of rapamycin activity an

98 e that Rvb2 is involved in an early stage of snoRNP biogenesis and may play a role in coupling snoRNA

99 ose that Nopp140 functions as a chaperone of snoRNPs in yeast and vertebrate cells.

100 ed on studies in yeast is that each class of snoRNPs is composed of a unique set of proteins.

101 tegral component of the box H + ACA class of snoRNPs, which function to target the enzyme to its site

102 The two major classes of snoRNPs, box H/ACA and box C/D, function in the pseudour

103 otein Nopp140 interacts with both classes of snoRNPs.

104 n leads to dissociation of the components of snoRNPs and the telomerase complex.

105 cription is arrested in nucleoli depleted of snoRNPs, raising the possibility of a feedback mechanism

106 MN complex in the assembly and metabolism of snoRNPs.

107 ay be involved in the binding and release of snoRNPs from pre-rRNA.

108 specific guide RNA component of the sRNP or snoRNP and the target rRNA.

109 essing snoRNP but is also present with other snoRNPs.

110 small nucleolar ribonucleoprotein particle (snoRNP) with the same four core proteins, NAP57 (also kn

111 small nucleolar ribonucleoprotein particles (snoRNP), a few of which are essential for processing pre

112 Small nucleolar ribonucleoprotein particles (snoRNPs) are essential cofactors in ribosomal RNA metabo

113 small nucleolar ribonucleoprotein particles (snoRNPs) are essential for the maturation and pseudourid

114 small nucleolar ribonucleoprotein particles (snoRNPs) in eukaryotes that are responsible for site spe

115 Small nucleolar ribonucleoprotein particles (snoRNPs) mainly catalyze the modification of rRNA.

116 small nucleolar ribonucleoprotein particles (snoRNPs) that are involved in posttranscriptional proces

117 small nucleolar ribonucleoprotein particles (snoRNPs) that play diverse and essential roles in riboso

118 inct distributions of U8 pre-snoRNAs and pre-snoRNP complexes in HeLa cell nuclear and cytoplasmic ex

119 res: (a) the existence of a protein-only pre-snoRNP complex containing five assembly factors and two

120 /D proteins in a partially reconstituted pre-snoRNP.

121 These proteins are key components of the pre-snoRNP complexes, but their exact role in box C/D snoRNP

122 probably reflects the conversion of the pre-snoRNP, where core protein-protein interactions are main

123 ng that they mediate the assembly of the pre-snoRNP.

124 y to be involved in the formation of the pre-snoRNP.

125 The distinct distribution of U8 pre-snoRNP complexes between the two cellular compartments t

126 vBL AAA(+) adenosine triphosphatase from pre-snoRNPs; and (d) a potential mechanism for preventing pr

127 NA, copurifies with the snR30/U17 processing snoRNP but is also present with other snoRNPs.

128 mplexes, including the U3 and U14 processing snoRNPs and several modifying snoRNPs examined.

129 embly complex coordinates snoRNA processing, snoRNP assembly, restructuring, and localization.

130 such as transcription, DNA damage response, snoRNP assembly, cellular transformation, and cancer met

131 CA small nucleolar (sno) ribonucleoparticle (snoRNP) biogenesis and assembly factor.

132 e box C/D small nucleolar ribonucleoprotein (snoRNP) assembly and ribosomal RNA processing.

133 erase and small nucleolar ribonucleoprotein (snoRNP) complexes.

134 of the U3 small nucleolar ribonucleoprotein (snoRNP) from the yeast Saccharomyces cerevisiae.

135 of the U3 small nucleolar ribonucleoprotein (snoRNP) is central to the events surrounding pre-rRNA pr

136 The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that gener

137 LA1 H/ACA small nucleolar ribonucleoprotein (snoRNP) particle that guides SL psi(28) formation.

138 of H/ACA small nucleolar ribonucleoprotein (snoRNP) particles is mutated in X-linked recessive DC.

139 enzymatic small nucleolar ribonucleoprotein, snoRNP) are frequently overexpressed in both murine and

140 ox H/ACA small nucleolar ribonucleoproteins (snoRNPs) and sequences in other eukaryotic RNAs target s

141 Box C/D small nucleolar ribonucleoproteins (snoRNPs) contain four core proteins: fibrillarin, Nop56,

142 box C/D small nucleolar ribonucleoproteins (snoRNPs) involves the sequential recruitment of core pro

143 class of small nucleolar ribonucleoproteins (snoRNPs) is primarily responsible for catalyzing the iso

144 grity of small nucleolar ribonucleoproteins (snoRNPs).

145 ox H/ACA small nucleolar ribonucleoproteins (snoRNPs).

146 NPs) and small nucleolar ribonucleoproteins (snoRNPs)], which are conserved from archaea to eukaryote

147 otein (U1-snRNP) and U3-small nucleolar RNP (snoRNP) in apoptotic cells.

148 Two core small nucleolar RNP (snoRNP) proteins, Nop1p (fibrillarin in vertebrates) and

149 a autoantigens such as small nucleolar RNPs (snoRNP) also associate with phosphoproteins in response

150 The box C/D small nucleolar RNPs (snoRNPs) are essential for the processing and modificati

151 The box C/D small nucleolar RNPs (snoRNPs) are essential for the processing and modificati

152 majority of box H/ACA small nucleolar RNPs (snoRNPs) have been shown to direct site-specific pseudou

153 cleolus and are called small nucleolar RNPs (snoRNPs), while in archaea they are known as small RNPs

154 for association between TbMTr1 and the SLA1 snoRNP but does not affect U1 small nuclear RNA methylat

155 eudouridylase activity is dependent on snR81 snoRNP in vivo.

156 tein complexes, including ribosomes, snRNPs, snoRNPs, telomerase, microRNAs, and long ncRNAs.

157 ing blockage experiments further reveal that snoRNP proteins bind specifically at the spliceosomal C1

158 We suggest that snoRNP assembly involves an intricate series of interact

159 The snoRNP-associated phosphoprotein complex is composed of

160 NA helicase activity but may be aided by the snoRNP core proteins.

161 de region, function as binding sites for the snoRNP proteins including the enzymatic subunit fibrilla

162 e interaction of TgNoAP1 with factors of the snoRNP and R2TP complexes indicates this protein has a r

163 Our data imply that the snoRNP assembly factor NUFIP can regulate the interactio

164 and/or recruitment of these proteins to the snoRNP complex is induced by multiple apoptotic stimuli

165 The snoRNPs mediate these functions through direct base pair

166 fficient association and dissociation of the snoRNPs, however, how such hierarchy is established has

167 ation and the structural organization of the snoRNPs.

168 protein Nopp140 (Srp40p) associates with the snoRNPs.

169 Autoantibodies to snoRNP components were more frequent in patients with di

170 as well as many non-snoRNP factors linked to snoRNP assembly (TIP48, TIP49, Nopp140), RNA processing

171 ins why the access of substrate sequences to snoRNPs is facile and how uridine selection may occur wh

172 romyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and i

173 veals that both proteins are critical for U3 snoRNP function in pre-18S rRNA processing at the A0, A1

174 However, as with other U3 snoRNP-specific proteins, neither Imp3p nor Imp4p is req

175 Thus, the role in processing of the U3 snoRNP can be separated into cleavage at the A0 site, wh

176 0p is a specific protein component of the U3 snoRNP in yeast.

177 larin-positive patients suggests that the U3 snoRNP particle is a source of immunogenic/antigenic mat

178 novel protein components specific to the U3 snoRNP with critical roles in pre-rRNA cleavage events.

179 sly undescribed protein components of the U3 snoRNP, representing the first snoRNP components identif

180 The U3 snoRNP, via base pairing, and its associated proteins, a

181 oteins that physically associate with the U3 snoRNP-specific protein, Mpp10p, we have identified Imp3

182 and for antibodies to fibrillarin and the U3 snoRNP-specific proteins Mpp10 and hU3-55K.

183 further elucidate the composition of the U3 snoRNP.

184 duction and impairs cleavage at the three U3 snoRNP-dependent sites: A0, A1, and A2.

185 ibodies to protein components specific to U3 snoRNP, particularly Mpp10.

186 ces on both strands of the analog of the U65 snoRNP pseudouridylation pocket in HJ1 pair with its sub

187 U8 snoRNP is required for accumulation of mature 5.8S and 2

188 ursor complex suggests that the mammalian U8 snoRNP is exported during biogenesis.

189 t of a small nucleolar ribonucleoprotein (U8 snoRNP) required for accumulation of mature 5.8S and 28S

190 We previously demonstrated that U8 snoRNP is essential for processing of both 5.8 and 28 S

191 Here we show that the U8 snoRNP is also restructured, suggesting that this may oc

192 es of U8 RNA show that this region of the U8 snoRNP is necessary for processing of pre-rRNA but not s

193 proteins comprising, or recruited by, the U8 snoRNP modulate the efficiency of cleavage.

194 Analysis of in vivo snoRNP assembly indicated that Nop56p was stably associa

195 ticular, the dense fibrillar component where snoRNPs are localized.

196 n of the Psi in 5.8S rRNA is associated with snoRNP activity, the pseudouridylation of 5S rRNA is not

197 rect evidence linking SUMO modification with snoRNP function.

198 lay a role in coupling snoRNA synthesis with snoRNP assembly and localization.

199 sociation of the phosphoprotein complex with snoRNPs in cells treated with the xenobiotic agent mercu

200 sociation of phosphorylated SR proteins with snoRNPs in cells undergoing apoptosis suggests that the

201 Monoclonal antibodies reactive with snoRNPs precipitated a phosphoprotein complex (pp42, pp3