ライフサイエンスコーパス: sura

1 hway that functions in parallel with that of SurA.

2 y complements the in vivo function of intact SurA.

3 round lacking the periplasmic folding factor SurA.

4 four periplasmic proteins was independent of SurA.

5 V37G), significantly reduced the activity of SurA.

6 peptidyl-prolyl isomerase (PPIase) domain of SurA.

7 of the periplasmic chaperone Skp but not by SurA.

8 Skp and DegP is amplified in the absence of SurA.

9 bility could be attributed to the absence of SurA.

10 a ribosome-binding bacterial chaperone, and SurA, a periplasmic chaperone in Gram-negative bacteria.

11 at the POTRA 1 domain of BamA interacts with SurA, a periplasmic chaperone required for the assembly

12 SurA, a periplasmic protein of Escherichia coli, has seq

13 We present evidence that SurA, a periplasmic protein with peptidyl-prolyl isomera

14 designed to target the codon for Pro-196 of SuRA, a tobacco acetolactate synthase (ALS) gene.

15 nvestigate the role of the PPIase domains in SurA activity, we deleted one or both PPIase domains fro

16 n the mouse bladder resulted in depletion of SurA after invasion of the bacteria into the superficial

17 Depletion of SurA alone results in a marked decrease in outer membran

18 onpolar-proline amino acids emerges for both SurA and a SurA "core domain," which remains after delet

19 M by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure successful OMP deli

20 The data suggest that SurA and BamA POTRA 1 domain function in concert to assi

21 protein interactions between the periplasmic SurA and DegP chaperones and either the EspP-beta or Esp

22 shortened relative to the trigger factor and SurA and in that PrsA is found to dimerize in a unique f

23 lations to map the client binding site(s) on SurA and interrogate the role of conformational dynamics

24 leted one or both PPIase domains from E.coli SurA and investigated the ability of the resulting prote

25 inities in the range of 1-14 microm for both SurA and its core domain.

26 retion of EspP was moderately reduced in the surA and skp mutant strains but severely impaired in the

27 tly of commonly used periplasmic chaperones, SurA and Skp.

28 ell overlaps with the periplasmic chaperones SurA and Skp.

29 nus interact with the periplasmic chaperones SurA and Skp.

30 the tobacco acetolactate synthase genes (ALS SuRA and SuRB), for which specific mutations are known t

31 the multifaceted functionalities of Skp and SurA and the fine-tuned balance between conformational f

32 esistance to high iron concentrations, while surA and tolB mutations grew poorly on high iron media.

33 The remaining PM(s) mutants (surA and tolB), as well as the two PmrA-regulated gene (

34 Furthermore, we demonstrate that SurA and YaeT interact directly in vivo.

35 and CFTR), an endogenous plant gene (tobacco SuRA), and a chromosomally integrated EGFP reporter gene

36 herichia coli periplasmic chaperones Skp and SurA, and BamA, the central subunit of the BAM complex,

37 n synthetic phenotypes, suggesting that Skp, SurA, and DegP are functionally redundant.

38 ggest that the functional redundancy of Skp, SurA, and DegP lies in the periplasmic chaperone activit

39 t the core domain is key to OMP expansion by SurA, and uncover a role for SurA PPIase domains in limi

40 o distinct groups of OMPs that follow either SurA- and lipopolysaccharide-dependent (OmpF/C) or -inde

41 In Escherichia coli, FkpA, PpiA, PpiD, and SurA are the four known periplasmic cis-trans prolyl iso

42 (the Bam complex) and a molecular chaperone (SurA) are both necessary and sufficient to promote the c

43 odalton protein (Skp) and survival factor A (SurA) are essential players in outer membrane protein (O

44 demonstrated that null mutations in skp and surA, as well as in degP and surA, result in synthetic p

45 We conclude that SurA assists in the folding of certain secreted proteins

46 s, and energetics that underpin both Skp and SurA associations with OMPs have remained largely unreso

47 ing three revertants that were obtained in a surA background, an alteration of N230Y was located 16 r

48 rected OmpF315 assembly at 42 degrees C in a surA(+) background, indicating that the two different ph

49 We further reveal that Skp and SurA bind their substrate in a fine-tuned thermodynamic

50 m the EspP passenger domain blocked DegP and SurA binding to the passenger domain.

51 ional dynamics and thermodynamics of Skp and SurA binding to unfolded OmpX and explore their disaggre

52 SurA binds as a monomer to the heptapeptide in an extend

53 The results suggest that SurA binds BAM at its soluble POTRA-1 domain, which may

54 d the yfgL background were used to show that SurA binds to YaeT (or another complex member) without g

55 r experimental data support a model in which SurA binds uOMPs in a groove formed between the core and

56 The absence of SurA blocks the assembly pathway and leads to accumulati

57 elivered to BAM by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure succe

58 o interact with uOMPs and that more than one SurA can bind a uOMP at a time.

59 only binding energy, the mechanism by which SurA carries out these two functions is not well-underst

60 T), and bioinformatics analyses we show that SurA client binding is mediated by two binding hotspots

61 otein profile, synthetic lethality with both surA::Cm and deltafkpA::Cm strains, and sensitivity to a

62 and deltanlpB are synthetically lethal with surA::Cm, which encodes a periplasmic chaperone and PPIa

63 E. coli SurA comprises a core domain and two peptidylprolyl isom

64 Escherichia coli SurA comprises three domains: a core and two PPIase doma

65 SurA consists of a substantial N-terminal region, two it

66 by this success, we created three additional SurA constructs, each containing a disulfide bond at dif

67 ch motifs in the client proteins, leading to SurA core/P1 domain rearrangements and expansion of clie

68 line amino acids emerges for both SurA and a SurA "core domain," which remains after deletion of a pe

69 to the core/P1 domains than suggested in the SurA crystal structure.

70 YaeT complex and the periplasmic chaperones SurA, DegP, and Skp.

71 mE mutant background, the absence of BamB or SurA does not affect BamA beta-barrel folding.

72 Overexpression of SurA does not restore LptD levels in a Deltaskp Deltafkp

73 effect on protein activity, indicating that SurA does not undergo large-scale conformational change

74 ses, ruling out a simple correlation between SurA domain architecture and these properties of OMP seq

75 bstrates bind in a cradle formed between the SurA domains, with structural flexibility between domain

76 operons encode LPS biosynthetic genes, while surA encodes a periplasmic cis-trans prolyl isomerase im

77 results demonstrate that the core domain of SurA endows its generic chaperone ability, while the pre

78 The periplasmic molecular chaperone protein SurA facilitates correct folding and maturation of outer

79 of surA rpoS double mutants, suggesting that SurA foldase activity is important for the proper assemb

80 of a complex between the dodecapeptide and a SurA fragment lacking the second PPIase domain at 3.4 A

81 ations in the rfa and rfb operons and in the surA gene all abolished the ability of UTI89 to suppress

82 Although the surA gene had been identified in a screen for mutants th

83 Deletion of the surA gene in Escherichia coli leads to a decrease in out

84 Escherichia coli SurA has a core domain and two peptidylprolyl isomerase

85 The peptide binding specificity of SurA has been characterized using phage display of hepta

86 Here we show that while SurA homologues in early proteobacteria typically contai

87 autotransporter is associated with BamA and SurA; (iii) the stalled intimin is decorated with large

88 educed upon depletion of a wild-type copy of surA in both instances.

89 presence of two PPIase domains is common in SurA in later proteobacteria, implying an evolutionary a

90 assembly defects, supporting the key role of SurA in outer membrane biogenesis.

91 e conservation of multiple PPIase domains in SurA in proteobacteria.

92 vive in stationary phase, the role played by SurA in stationary-phase survival remained unknown.

93 phide bond engineering in an attempt to trap SurA in the act of OMP delivery to BAM, and solve cryoEM

94 In this study, we investigated the role of SurA in the UPEC pathogenic cascade.

95 ane proteins (OmpA, OmpF, and LamB) requires SurA in vivo, while the folding of four periplasmic prot

96 The results show that wild-type SurA inhibits the aggregation of both OMPs, as do the cy

97 correlated with improved BamA folding, BamA-SurA interactions, and LptD (lipopolysaccharide transpor

98 SurA interacts preferentially (>50-fold) with in vitro s

99 are components of the same pathway and that SurA is a component of a separate pathway.

100 SurA is a conserved ATP-independent periplasmic chaperon

101 SurA is a periplasmic peptidyl-prolyl isomerase required

102 SurA is a periplasmic prolyl isomerase/chaperone that fa

103 We demonstrate that SurA is involved in the conversion of unfolded monomers

104 riplasmic peptidyl-prolyl isomerase (PPIase) SurA is involved in the maturation of outer membrane por

105 Our data argue that SurA is required within bladder epithelial cells for UPE

106 SurA is the most important member of this network, both

107 Based on these results, we suggest that SurA is the primary chaperone responsible for the peripl

108 SurA is the primary periplasmic molecular chaperone that

109 By contrast, SurA is unable to release tOmpA from Skp, providing dire

110 d intimin is decorated with large amounts of SurA; (iv) the stalled autotransporter is not degraded b

111 The Deltaskp surA::kan combination has a bacteriostatic effect and le

112 leads to filamentation, while the degP::Tn10 surA::kan combination is bactericidal.

113 ormal, but in contrast to UTI89, UTI89/pDH15 surA::kan formed intracellular collections that containe

114 er these conditions, invasion by UTI89/pDH15 surA::kan was normal, but in contrast to UTI89, UTI89/pD

115 In a murine cystitis model, UTI89 surA::kan was unable to persist in the urinary tract.

116 Complementation of UTI89 surA::kan with a plasmid (pDH15) containing surA under t

117 Here we show that a variant of SurA lacking both parvulin-like domains exhibits a PPIas

118 Moreover, we found that surA mutants are qualitatively indistinguishable from yf

119 S. flexneri skp and surA mutants failed to form plaques in Henle cell monola

120 here demonstrate that the survival defect of surA mutants is due to their inability to grow at elevat

121 The results reveal insights into SurA-OMP recognition and the mechanism of activation for

122 igated the effect of two chaperones, Skp and SurA, on the folding kinetics of the OMP, PagP.

123 This work demonstrates that SurA operates in a distinct fashion compared to other ch

124 rial periplasmic chaperone Skp, but not with SurA or SecB, resulted in enhanced levels of both forms

125 kp function to rescue OMPs that fall off the SurA pathway.

126 The periplasmic chaperone SurA plays a key role in outer membrane protein (OMP) bi

127 MP expansion by SurA, and uncover a role for SurA PPIase domains in limiting the extent of expansion.

128 suggest that the chaperone-like function of SurA preferentially facilitates maturation of outer memb

129 The ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) fr

130 first PPIase domain of the Escherichia coli SurA protein at 1.3 A resolution, and of a complex betwe

131 The Escherichia coli SurA protein is a periplasmic molecular chaperone that f

132 substantial structural rearrangement of the SurA protein.

133 SP, including TDE1658, a spirochete-specific SurA/PrsA ortholog.

134 Precisely how SurA recognises and binds its different OMP clients rema

135 Thus, SurA recognizes a peptide motif that is characteristic o

136 that disrupt the interaction between BAM and SurA result in outer membrane assembly defects, supporti

137 ions in skp and surA, as well as in degP and surA, result in synthetic phenotypes, suggesting that Sk

138 d the main periplasmic chaperone in E. coli, SurA, results in synthetic lethality.

139 In cultures of surA rpoS double mutants the survivors lysed as they att

140 maS had a survival defect similar to that of surA rpoS double mutants, suggesting that SurA foldase a

141 We demonstrate that SurA samples an array of conformations in solution in wh

142 oteins that are more readily digested (e.g., SurA) serve as more sensitive reporters of membrane inte

143 In contrast, SurA showed no effect on the observed folding rates of P

144 ant were indistinguishable from those in the surA single mutant.

145 s affected by known folding factors, such as SurA, Skp, and lipopolysaccharide, which have profound e

146 periplasmic chaperone network that contains SurA, Skp, DegP, PpiD, and FkpA.

147 the key structural features that define how SurA solubilizes uOMPs.

148 igger conformational changes in both BAM and SurA that enable transfer of the unfolded OMP to the BAM

149 SurA therefore asserts a recognition preference for arom

150 However, while the ability of SurA to bind and prevent tOmpA aggregation does not depe

151 nt, suggesting that Skp acts in concert with SurA to efficiently assemble LptD in E. coli.

152 Here, we conducted mutational studies on SurA to identify residues that are critical for function

153 single PPIase domain ablates the ability of SurA to prevent OmpT aggregation.

154 o PM, and transposon insertion sites include surA, tolB, and gnd.

155 surA::kan with a plasmid (pDH15) containing surA under the control of an arabinose-inducible promote

156 h to create a sparse ensemble of models of a SurA*uOMP complex.

157 We validated key structural features of the SurA*uOMP ensemble using independent scattering and chem

158 Our data suggest that SurA utilizes three distinct binding modes to interact w

159 The loss of activity in SurA(V37G) could be restored through the introduction of

160 Further characterization indicated that SurA(V37G) was structurally similar to, but less stable

161 One mutant, SurA(V37G), significantly reduced the activity of SurA.

162 al cells was disproportionately reduced when surA was genetically disrupted in the UPEC strain UTI89,

163 We tested whether SurA was involved in folding periplasmic and outer membr

164 e periplasmic folding factors DegP, Skp, and SurA were all required for IcsA localization and plaque

165 The gene for one such sRNA, SurA, which is located in the region between yndK and yn

166 ivery to periplasmic chaperones, for example SurA, which prevent aggregation.

167 lls lacking the major periplasmic chaperone, SurA, which, together with BamB, is thought to facilitat