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 r the catalytic activity of bacterial type I signal peptidase.

3 gion that contains the cleavage site for the 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 utions in the consensus site for cleavage by signal peptidase.

9 omycin, a selective inhibitor of lipoprotein signal peptidase.

10 peptide modulated alternate-site cleavage by signal peptidase.

11 omycin, a selective inhibitor of lipoprotein signal peptidase.

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

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

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

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

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

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

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

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

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

21 mnant signal peptides after their release by signal peptidase.

22 intain activity of the membrane-incorporated signal peptidase.

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

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

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

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

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

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

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

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

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

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

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

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

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

36 hese proteins perform redundant functions in signal peptidase activity.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

51 Type I signal peptidases are integral membrane proteins that fu

52 Prokaryotic signal peptidases are membrane-bound enzymes.

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

54 The multisubunit signal peptidase catalyzes the cleavage of signal peptid

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

100 Signal peptidase functions to cleave signal peptides fro

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

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

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

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

105 -144 and Ile-86 residues in Escherichia coli signal peptidase I (SPase) can change the specificity su

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

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

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

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

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

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

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

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

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

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

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

117 25-amino-acid leader peptide terminated by a signal peptidase I cleavage site.

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

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

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

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

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

123 Bacterial signal peptidase I is responsible for proteolytic proces

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

162 Since bacterial signal peptidase is capable of processing both prokaryot

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

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

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

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

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

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

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

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

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

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

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

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

175 Signal peptidases of prokaryotic organisms reside in the

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

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

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

179 termined by Edman degradation, demonstrating signal peptidase processing.

180 olytically removed from exported proteins by signal peptidase processing.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

206 903c) encodes the sole homolog of the type I signal peptidase (SPase).

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

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

209 A signal peptidase specifically required for the secretion

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

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

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

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

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

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

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

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

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

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

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

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

222 Signal peptidase, which removes signal peptides from pre

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