ライフサイエンスコーパス: sura

1 round lacking the periplasmic folding factor SurA.

2 four periplasmic proteins was independent of SurA.

3 V37G), significantly reduced the activity of SurA.

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

5 of the periplasmic chaperone Skp but not by SurA.

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

7 bility could be attributed to the absence of SurA.

8 hway that functions in parallel with that of SurA.

9 y complements the in vivo function of intact 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 n the mouse bladder resulted in depletion of SurA after invasion of the bacteria into the superficial

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

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

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

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

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

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

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

23 ell overlaps with the periplasmic chaperones SurA and Skp.

24 nus interact with the periplasmic chaperones SurA and Skp.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

69 SurA is a periplasmic peptidyl-prolyl isomerase required

70 SurA is a periplasmic prolyl isomerase/chaperone that fa

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

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

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

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

75 SurA is the primary periplasmic molecular chaperone that

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

94 substantial structural rearrangement of the SurA protein.

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

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

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

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

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

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

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

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

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

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

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

106 SurA therefore asserts a recognition preference for arom

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

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

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

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

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

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

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

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

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

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

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

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