PapD-like chaperones and pilus biogenesis

Seminars in Cell and Developmental Biology

Volumn 11, Issue 1, 2000, Pages 27-34

  Sauer, Frederic G ^a   Knight, Stefan D ^b   Waksman and, Gabriel J ^a   Hultgren, Scott J ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

Author keywords

Chaperone; Organelle biogenesis; Pilus; Protein folding

Indexed keywords

CHAPERONE; PAPD LIKE CHAPERONE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

BACTERIUM PILUS; BIOGENESIS; CELL ORGANELLE; CYTOPLASM; GRAM NEGATIVE BACTERIUM; NONHUMAN; PROTEIN ASSEMBLY; PROTEIN FOLDING; REVIEW;

NEGIBACTERIA;

EID: 0034488543     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1999.0348     Document Type: Article

References (46)

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3. PapD, a periplasmic transport protein in P-pilus biogenesis
4. FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria
5. Construction and expression of recombinant plasmids encoding type 1 or D-mannose-resistant pili from a urinary tract infection Escherichia coli isolate
6. P pili in uropathogenic E. coli are composite fibers with distinct fibrillar tips
7. Structural polymorphism of bacterial adhesion pili
8. Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins
9. The PapG protein is the α-D-galactopyranosyl-(1 → 4)-β-D-galactopyranosyl-binding adhesin of uropathogenic Escherichia coli
10. The gal(α 1-4)gal-specific tip adhesin of Escherichia coli P-fimbriae is needed for pyclonephritis to occur in the normal urinary tract
11. FimH adhesin of type I pili is assembled into a fibrillar tip structure in the Enterobacteriaceae
12. The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
13. Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits
14. Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper
15. Structural basis of pilus subunit recognition by the PapD chaperone
16. Periplasmic chaperone recognition motif of subunits mediates quaternary interactions in the pilus
17. The chaperone/usher pathway: A major terminal branch of the general secretory pathway
18. Outer membrane PapC molecular usher discriminately recognizes periplamic chaperone-pilus subunit complexes
19. The PapC usher forms an oligomeric channel: Implications for pilus biogenesis across the outer membrane
20. Ramifications of kinetic partitioning on usher-mediated pilus biogenesis
21. The sigmaE and Cpx regulatory pathways: Overlapping but distinct envelope stress responses
22. The sigma(E) and Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
23. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress inducible periplasmic protease DegP
24. PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA
25. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
26. NMR solution structure of the periplasmic chaperone FimC
27. X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli
28. Structural basis of chaperone function and pilus biogenesis
29. Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly
30. The immunoglobulin superfamily
31. Context is a major determinant of β-sheet propensity
32. Synthesis and conformational studies of peptides from E. coli pilus proteins recognized by the chaperone PapD
33. The Hsp70 and Hsp60 chaperone machines
34. Chaperonin function: Folding by unfolding
35. Chaperone-assisted self-assembly of pili independent of cellular energy
36. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
37. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly
38. Characterization of the Escherichia coli AF/R1 pilus operon: Novel genes necessary for transcriptional regulation and for pilus-mediated adherence
39. New tools in an old trade: CS1 pilus morphogenesis
40. Availability of the fibre subunit CsgA and the nucleator protein CsgB during assembly of fibronectin-binding curli is limited by the intracellular concentration of the novel lipoprotein CsgG
41. Components of the Salmonella flagellar export apparatus and classification of export substrates
42. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
43. Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD
44. Individual chaperones required for Yop secretion by Yersinia
45. YscB of Yersinia pestis functions as a specific chaperone for YopN
46. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia entercolitica forms a ring-shaped multimeric complex