ライフサイエンスコーパス: signal peptidase

1 d lsp (encoding the S. aureus prolipoprotein signal peptidase).

2 s a putative secreted protein, and SipW is a signal peptidase.

3 r the catalytic activity of bacterial type I signal peptidase.

4 sequence, with no evidence for processing by signal peptidase.

5 n, the signal sequence is cleaved from E1 by signal peptidase.

6 way and have their signal peptide removed by signal peptidase.

7 e (-3, -1) rule for substrate recognition by signal peptidase.

8 gion that contains the cleavage site for the signal peptidase.

9 utions in the consensus site for cleavage by signal peptidase.

10 omycin, a selective inhibitor of lipoprotein signal peptidase.

11 peptide modulated alternate-site cleavage by signal peptidase.

12 omycin, a selective inhibitor of lipoprotein signal peptidase.

13 dues, presumably the result of cleavage by a signal peptidase.

14 ecting Sec11p, an essential subunit of yeast signal peptidase.

15 t the endoplasmic reticulum (ER) membrane by signal peptidase.

16 suggesting that it may be removed by a novel signal peptidase.

17 ion system and a candidate for being the CTD signal peptidase.

18 regulatory role in addition to its role as a signal peptidase.

19 Astn1 and Astn2 as the endoplasmic reticulum signal peptidase.

20 s of this enzyme were consistent with type I signal peptidase.

21 y to globomycin, an inhibitor of lipoprotein signal peptidase.

22 , it seems unlikely that SipA functions as a signal peptidase.

23 culosis gene (lspA) that encodes lipoprotein signal peptidase.

24 mnant signal peptides after their release by signal peptidase.

25 intain activity of the membrane-incorporated signal peptidase.

26 tinguishes Imp1p and Imp2p from other type I signal peptidases.

27 Plastidic Type I Signal Peptidase 1 (Plsp1) is an integral thylakoid memb

28 he thylakoid integration of Plastidic type I signal peptidase 1 (Plsp1) using in vitro targeting assa

29 protein kinase 8) or Plsp1 (Plastidic type I signal peptidase 1), was replaced with the stop-transfer

30 used M. tuberculosis lacking prolipoprotein signal peptidase A (lspA), an enzyme required for lipopr

31 ptide cleavage of the nascent protein by the signal peptidase, a second COOH-terminal signal peptide

32 over, Spc2p, but not Spc1p, is important for signal peptidase activity and cell viability at high tem

33 at both Spc1p and Spc2p are nonessential for signal peptidase activity and growth of yeast cells and

34 ne, and two aspartic acids are important for signal peptidase activity by the Sec11p subunit of the y

35 least two of its subunits is sufficient for signal peptidase activity in vivo.

36 Surprisingly, we found that the signal peptidase activity of SipW was not required for s

37 t Spc3p is also required for cell growth and signal peptidase activity within the yeast endoplasmic r

38 g event is most likely independent of type I signal peptidase activity.

39 ears, however, to be important for efficient signal peptidase activity.

40 hese proteins perform redundant functions in signal peptidase activity.

41 rm a solid-surface biofilm but still retains signal peptidase activity.

42 strand RNA virus, is carried out by the host signal peptidase and a novel two-component viral protein

43 ified determinants in S. gordonii encoding a signal peptidase and an Eep-like zinc metalloprotease (l

44 o mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requi

45 ed a human cDNA clone that may function as a signal peptidase and have demonstrated that the function

46 ER signal peptidase subunits is required for signal peptidase and protein degradation activities in v

47 vide an example of a SP that is processed by signal peptidase and retrotranslocated to allow nuclear

48 n the ER lumen flanked by cleavage sites for signal peptidase and S1P.

49 rU, the only known dual-function, C-terminal signal peptidase and sortase.

50 Removal of the signal peptide by signal peptidase and the autocatalytic cleavage of the l

51 Amino acids critical to the eubacterial signal peptidases and Sec11p are, however, positioned si

52 nserted into the ER, undergoes processing by signal peptidase, and subsequently undergoes retrotransl

53 ding in an operon with sipW, which encodes a signal peptidase, and tasA, which encodes an antibiotic

54 The prepeptide is removed by a signal peptidase, and the propeptide is cleaved from the

55 re cleaved by endoplasmic reticulum-resident signal peptidase, and thus, are not present on mature me

56 Type I signal peptidases are integral membrane proteins that fu

57 Prokaryotic signal peptidases are membrane-bound enzymes.

58 For the signal peptidase assay, we inserted an SPase I cleavage

59 activity of SpsB, we named this factor SpbR (Signal peptidase b Regulator).

60 The multisubunit signal peptidase catalyzes the cleavage of signal peptid

61 ulation relative to untagged Rem and allowed signal peptidase cleavage but reduced its specific activ

62 ed with the presequence N terminus formed by signal peptidase cleavage in the vesicle lumen and the m

63 mine mechanisms that may lead to alternative signal peptidase cleavage including alternative translat

64 at the variants are generated by alternative signal peptidase cleavage of the nascent polypeptide at

65 e attributed to genetic codon degeneracy and signal peptidase cleavage preferences.

66 Mutations in the signal peptidase cleavage sequence of VirB2 propilin cau

67 g, Lys, and Gln) immediately adjacent to the signal peptidase cleavage site (Ala-X-Ala) that are not

68 ndergoes proteolytic cleavage at a consensus signal peptidase cleavage site after residue 259, yieldi

69 e analysis allowed the identification of the signal peptidase cleavage site and revealed that the 31-

70 Disruption of the region between the signal peptidase cleavage site and the LPNTG domain resu

71 -glycated); by contrast, human Nrf3 lacked a signal peptidase cleavage site between its c region and

72 Alteration of the predicted signal peptidase cleavage site by mutagenesis blocked ge

73 We showed that lack of a signal peptidase cleavage site is not responsible for th

74 peptide of 24 amino acids ending in a type I signal peptidase cleavage site of Leu-Ala-Ala.

75 gion (residues 24-39) was found to contain a signal peptidase cleavage site that is responsible for p

76 ng were enhanced by altering its lipoprotein signal peptidase cleavage site to mimic that of the mure

77 a potential signal sequence and a consensus signal peptidase cleavage site were identified, indicati

78 library, +1, +3 and +12 downstream from the signal peptidase cleavage site.

79 id signal peptide, followed by a lipoprotein signal peptidase cleavage site.

80 roximately 60 amino acids from the predicted signal peptidase cleavage site.

81 peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site.

82 alanine (apoM(Q22A)) introduces a functional signal peptidase cleavage site.

83 peptide, followed by an L-X-Y-C lipoprotein signal peptidase cleavage site.

84 lyses revealed that the mutations influenced signal peptidase cleavage specificity, resulting in an i

85 cDNA library instead, the N-terminal site of signal peptidase cleavage upon protein secretion was pre

86 ylation at Asn(1) did not affect the site of signal peptidase cleavage.

87 generation of the amino terminus of prM via signal peptidase cleavage.

88 veral type II membrane signal peptides after signal peptidase cleavage.

89 Instead constitutively active signal peptidase cleaves RsiV at site-1 in a lysozyme-de

90 type I SP with two catalytic subunits is the signal peptidase complex (SPC) in the mammalian endoplas

91 mouse iRhom2 are non-canonical substrates of signal peptidase complex (SPC), the protease that remove

92 t processing of their signal sequence by the signal peptidase complex (SPC).

93 In the endoplasmic reticulum, the signal peptidase complex cleaves off a large N-terminal

94 In contrast, our data show that the signal peptidase complex from the endoplasmic reticulum

95 o wild type yeast cells, indicating that the signal peptidase complex missing at least two of its sub

96 three characterized subunits comprising the signal peptidase complex of the yeast Saccharomyces cere

97 ied the DNF1 gene as encoding a subunit of a signal peptidase complex that is highly expressed in nod

98 le (SRP), SRP receptors, the translocon, the signal peptidase complex, and over 100 other genes with

99 Host factors, including a signal peptidase complex, probably associate with the US

100 Two subunits of the mammalian signal peptidase complex, SPC12 and SPC25, share similar

101 activity by the Sec11p subunit of the yeast signal peptidase complex.

102 gen fixation via proteolytic processing by a signal peptidase complex.

103 or cell growth, signal peptide cleavage, and signal peptidase-dependent protein degradation.

104 teins are cleaved at a very specific site by signal peptidase during posttranslational translocation

105 opolysaccharide synthesis), sipW (encoding a signal peptidase), ecsB (encoding an ABC transporter sub

106 partial conservation of motifs of the type I signal peptidase family proteins, SipA lacks the highly

107 reas both subunits are members of the type I signal peptidase family, they exhibit nonoverlapping sub

108 xpression, suggesting that LepB is the major signal peptidase for protein secretion and supporting ou

109 Many type I signal peptidases from eubacterial cells appear to conta

110 Signal peptidase functions to cleave signal peptides fro

111 subtilis SinR-regulated genes, including the signal peptidase gene sipW near the sinIR locus and the

112 utations that reduced Rem or Env cleavage by signal peptidase greatly reduced SP levels and functiona

113 o in-frame AUGs and a suboptimal context for signal peptidase hydrolysis at the primary cleavage site

114 Using a novel signal peptidase I (SPase I) cleavage assay, we show tha

115 -144 and Ile-86 residues in Escherichia coli signal peptidase I (SPase) can change the specificity su

116 Signal peptidase I (SpI) cleavage sites were found in 46

117 d R. typhi have been demonstrated to possess signal peptidase I activity in Escherichia coli preprote

118 Finally, Gly-272 is essential for signal peptidase I activity, consistent with it being lo

119 the evidence suggests that it is cleaved by signal peptidase I and a 19-residue C-terminal domain is

120 ey P3 substrate specificity determinants for signal peptidase I and demonstrates the power of the flu

121 All these data suggest that signal peptidase I and LexA-like proteases are closely r

122 Sequence analysis revealed that the signal peptidase I and LexA-like proteases show sequence

123 ues serine 38 and lysine 76 of S. pneumoniae signal peptidase I are critical for enzyme activity and

124 erved region, Box E, of the Escherichia coli signal peptidase I are critical for maintaining a functi

125 imilar to LexA-like proteases, S. pneumoniae signal peptidase I catalyzes an intermolecular self-clea

126 etwork trained to identify the most probable signal peptidase I cleavage site of secreted proteins.

127 election criteria included the presence of a signal peptidase I cleavage site, a predicted beta-barre

128 25-amino-acid leader peptide terminated by a signal peptidase I cleavage site.

129 BBA74 is posttranslationally modified by signal peptidase I cleavage to a mature 25-kDa protein.

130 xamined to date, yeast Sec11p, is related to signal peptidase I from bacteria.

131 roteases including calpain, metacaspase, and signal peptidase I have been implicated to be central me

132 proposed for the catalytic dyad mechanism of signal peptidase I in which the general base Lys-145 is

133 to incorporate full-length Escherichia coli signal peptidase I into phospholipid vesicles.

134 Bacterial signal peptidase I is responsible for proteolytic proces

135 we have cloned, expressed, and purified the signal peptidase I of gram-positive Streptococcus pneumo

136 With the criteria of a signal peptidase I or II cleavage site or a predicted tr

137 amino acids that is homologous to bacterial signal peptidase I proteins.

138 of the consensus endoplasmic reticulum (ER) signal peptidase I site within exon 3 (UL37x3) were repl

139 was inhibited by a C(16) compound targeting signal peptidase I, but not by a C(1) compound known to

140 e protein (Bmp), a previously characterized, signal peptidase I-processed protein.

141 to LexA-like proteases and Escherichia coli signal peptidase I.

142 s identified as a substrate of S. pneumoniae signal peptidase I.

143 yme in the ER contains proteins unrelated to signal peptidase I.

144 rotein secretion by altering the activity of signal peptidase IB.

145 al peptides and predicted cleavage sites for signal peptidase II (Ala-Ala-Ala downward arrowCys).

146 Posttranslational processing requires a signal peptidase II (LspA) that removes the signal pepti

147 The signal sequence is then cleaved by signal peptidase II (LspA) to give an N-terminal S-diacy

148 protein diacylglyceryl transferase (lgt) and signal peptidase II (lspA).

149 spite the absence of an archaeal lipoprotein signal peptidase II (SPase II) homologue, the SPase II i

150 poprotein signal peptide recognition site of signal peptidase II (SpII).

151 Inhibition of signal peptidase II by globomycin resulted in failure to

152 ical signal sequence ending with a consensus signal peptidase II cleavage site characteristic of bact

153 for the invariant Cys-15 residue within the signal peptidase II cleavage site could not be visualize

154 in encoded by ORF113 was predicted to have a signal peptidase II cleavage site, and globomycin inhibi

155 contains a signal sequence with a potential signal peptidase II cleavage site, and has 26% identity

156 eated, placing the epitope downstream of the signal peptidase II cleavage site.

157 tment of cells producing native OPH with the signal peptidase II inhibitor globomycin resulted in acc

158 Consistent with this observation, a signal peptidase II inhibitor, globomycin, was found to

159 The MnuA protein contained a prolipoprotein signal peptidase II recognition sequence along with an e

160 The N terminus has a signal peptidase II recognition sequence, cleavage of wh

161 er membrane lipoprotein that is processed by signal peptidase II.

162 ence for the prolipoprotein cleavage site of signal peptidase II.

163 ocessing by globomycin, a known inhibitor of signal peptidase II.

164 showed that the connexins were processed by signal peptidase immediately downstream of their first t

165 to be processed by the endoplasmic reticulum signal peptidase implying that the peptidase is closely

166 Rem cleavage by signal peptidase in the ER is necessary for MMTV-SP func

167 n the notion that Plsp1 is a redox-dependent signal peptidase in the thylakoid lumen.

168 , PhrE, and PhrC suggested a role for type I signal peptidases in the processing of the Phr preinhibi

169 atures of phospholipid vesicles incorporated signal peptidase, including the effect of lipid concentr

170 rotein and have renamed lirL (prolipoprotein signal peptidase inhibitor resistance lipoprotein).

171 eavage inhibits the production of prM by the signal peptidase, inhibits particle release, and elimina

172 In addition, we find that signal peptidase is able to cleave after phenylalanine a

173 (SPase) can change the specificity such that signal peptidase is able to cleave pro-OmpA nuclease A i

174 These data provide the first evidence that a signal peptidase is bifunctional and that SipW has a reg

175 Since bacterial signal peptidase is capable of processing both prokaryot

176 s (HCV) E2-p7-NS2 precursor mediated by host signal peptidase is relatively inefficient, resulting in

177 tributes to the high fidelity of cleavage of signal peptidase is the Ile-144 residue.

178 via the novel mechanism of inhibiting type I signal peptidase, is broader than previously believed an

179 The type I signal peptidase lepB genes from Rickettsia rickettsii a

180 n of the arylomycin target, bacterial type I signal peptidase LepB, is a mechanism of unstable arylom

181 which prevent SrtA cleavage mediated by the signal peptidase LepB2.

182 f the CTD and deletion of porU, a C-terminal signal peptidase linked to T9SS-mediated secretion.

183 Deleting the lipoprotein signal peptidase (lsp) gene in Streptomyces coelicolor r

184 rent bacterial species, and requires type II signal peptidase (Lsp) mediated cleavage of the N-termin

185 The signal peptide is cleaved by lipoprotein signal peptidase (Lsp) to leave the lipid-modified cyste

186 aved of their signal peptides by lipoprotein signal peptidase (Lsp).

187 tial type II signal peptidase prolipoprotein signal peptidase (LspA), is ineffective against wild-typ

188 ion at a terminal residue of E2 to block the signal peptidase-mediated cleavage of this junction site

189 tein transferase), and lepB (encoding type I signal peptidase), monitored by real-time quantitative r

190 itro analyses indicate that none of the five signal peptidases of B. subtilis (SipS, SipT, SipU, SipV

191 Signal peptidases of prokaryotic organisms reside in the

192 This subpopulation was accessible to signal peptidase on ribosome-associated polypeptides lon

193 peptides of membrane proteins are cleaved by signal peptidase once the nascent proteins reach the end

194 was used to show that a signal sequence for signal peptidase processing, when present in the viral c

195 termined by Edman degradation, demonstrating signal peptidase processing.

196 olytically removed from exported proteins by signal peptidase processing.

197 omycin, which inhibits the essential type II signal peptidase prolipoprotein signal peptidase (LspA),

198 nce of a suitable -3,-1 amino acid motif for signal peptidase recognition.

199 ese results indicate that the prolipoprotein signal peptidase requires a glyceride modified cysteine

200 of an internal signal peptide presumably by signal peptidase resident in the endoplasmic reticulum.

201 h genetic and gene expression tests, the non-signal peptidase role of SipW was found to activate biof

202 The membrane-bound signal peptidase showed high activity on a designed subs

203 showing that residues comprising the type I signal peptidase signature in the two catalytic subunits

204 A putative signal peptidase, SipA (also called LepA), has been iden

205 ccessfully isolated Bacillus subtilis type I signal peptidase (SipS) and a truncated version lacking

206 n B. subtilis cells unable to synthesize the signal peptidase SipW, TasA is not secreted, nor is it i

207 vestigated the role of the Bacillus subtilis signal peptidase, SipW, which has a unique role in formi

208 type II transmembrane protein with putative signal peptidase sites in its transmembrane domain, and

209 roteolytic processing by two host proteases: signal peptidase (SP) and the intramembrane-cleaving pro

210 Signal peptidase (SP) is an enzyme with a well defined r

211 Type I signal peptidase (SPase I) catalyzes the cleavage of the

212 Type I signal peptidase (SPase I) catalyzes the hydrolytic clea

213 Type I signal peptidase (SPase I) is an integral membrane Ser/L

214 In this study, we show that a type I signal peptidase (SPase I) is responsible for this proce

215 Lipoprotein processing by the type II signal peptidase (SPase II) is known to be critical for

216 iant cysteine residue at the junction of the signal peptidase (Spase) cleavage site along with a well

217 y demonstrated that Streptococcus pneumoniae signal peptidase (SPase) I catalyzes a self-cleavage to

218 Signal peptidase (SPase) I is responsible for the cleava

219 Signal peptidase (SPase) I is responsible for the cleava

220 inhibitors of the essential type I bacterial signal peptidase (SPase) may be more specific and thus l

221 s other bacteria, is dependent on the type I signal peptidase (SPase)-mediated cleavage of the N-term

222 ral event in protein secretion is the type I signal peptidase (SPase)-mediated cleavage of the N-term

223 903c) encodes the sole homolog of the type I signal peptidase (SPase).

224 We recently showed that type II signal peptidase (SPaseII) encoded by lspA is the target

225 Type I signal peptidases (SPases) cleave signal peptides from p

226 A signal peptidase specifically required for the secretion

227 TPP is homologous to Escherichia coli type I signal peptidase (SPI) called LepB.

228 Type I signal peptidases (SPs) comprise a family of structurall

229 and purification of the two known S. aureus signal peptidases, SpsA and SpsB, demonstrated that only

230 ategy is exploited in the present study with signal peptidase SpsB from Staphylococcus aureus.

231 t SpbR physically associates with the type I signal peptidase SpsB, which cleaves LtaS, the polymeras

232 ws that Ile-144 and Ile-86 contribute to the signal peptidase substrate specificity and that Ile-144

233 SPC3 gene encoding the homolog to mammalian signal peptidase subunit SPC22/23.

234 This indicates that only a subset of the ER signal peptidase subunits is required for signal peptida

235 1 (Plsp1) is an integral thylakoid membrane signal peptidase that requires an intramolecular disulfi

236 y, SafA is a membrane-imbedded antagonist of signal peptidase that safeguards and maintains membrane

237 e we provide evidence that after cleavage by signal peptidase, the signal peptide is further processe

238 slocon, and that this mispositioning enabled signal peptidase to access the cleavage sites.

239 east alpha-factor cDNA, using the yeast KEX2 signal peptidase to release the processed enzyme into th

240 eptide substrate into the active site of the signal peptidase using the known position of the beta-la

241 A putative lipoprotein signal peptidase was encoded by an adjacent ORF, lspA, a

242 Signal peptidase, which removes signal peptides from pre

243 epresses lspB, a gene encoding a lipoprotein signal peptidase whose expression appears detrimental fo