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Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation.

Kawamura T, Le LU, Zhou H, Dahlquist FW
J Mol Biol 365 1130-42 (2007)
Cited: 11 times
EuropePMC logo PMID: 17109885

Abstract

Pyelonephritis-associated pili (pap) allow uropathogenic Escherichia coli to bind to epithelial cells and play an important role in urinary tract infection. Expression of pap is controlled by a phase-variation mechanism, based on the two distinct heritable states that are the result of adenine N6-methylation in either of the two GATC sequences in its regulatory region. The methylation status of these two sequences is sensed by the action of two proteins, Lrp and PapI, and they play a central role in determining pap gene expression in both phase-ON and phase-OFF cells. We used modern NMR techniques to determine the solution structure and backbone dynamics of PapI. We found its overall fold resembles closely that of the winged helix-turn-helix family of DNA-binding proteins. We determined that PapI possesses its own DNA-binding activity, albeit non-sequence-specific, independent of Lrp. PapI appears to bind to DNA with a K(d) in the 10 microM range. Possible mechanisms by which PapI might participate in the regulation of the pap operon are discussed in light of these new findings.

Articles - 2htj mentioned but not cited (2)

  1. Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation. Kawamura T, Le LU, Zhou H, Dahlquist FW. J Mol Biol 365 1130-1142 (2007)
  2. Solution NMR structure of the plasmid-encoded fimbriae regulatory protein PefI from Salmonella enterica serovar Typhimurium. Aramini JM, Rossi P, Cort JR, Ma LC, Xiao R, Acton TB, Montelione GT. Proteins 79 335-339 (2011)


Reviews citing this publication (1)

  1. A Thermosensitive, Phase-Variable Epigenetic Switch: pap Revisited. Zamora M, Ziegler CA, Freddolino PL, Wolfe AJ. Microbiol Mol Biol Rev 84 (2020)

Articles citing this publication (8)

  1. The role of high affinity non-specific DNA binding by Lrp in transcriptional regulation and DNA organization. Peterson SN, Dahlquist FW, Reich NO. J Mol Biol 369 1307-1317 (2007)
  2. Regulatory interplay between pap operons in uropathogenic Escherichia coli. Totsika M, Beatson SA, Holden N, Gally DL. Mol Microbiol 67 996-1011 (2008)
  3. Solution structure of a complex of the histidine autokinase CheA with its substrate CheY. Mo G, Zhou H, Kawamura T, Dahlquist FW. Biochemistry 51 3786-3798 (2012)
  4. The design involved in PapI and Lrp regulation of the pap operon. Kawamura T, Vartanian AS, Zhou H, Dahlquist FW. J Mol Biol 409 311-332 (2011)
  5. Lrp-DNA complex stability determines the level of ON cells in type P fimbriae phase variation. Graveline R, Mourez M, Hancock MA, Martin C, Boisclair S, Harel J. Mol Microbiol 81 1286-1299 (2011)
  6. Leucine-responsive regulatory protein Lrp and PapI homologues influence phase variation of CS31A fimbriae. Graveline R, Garneau P, Martin C, Mourez M, Hancock MA, Lavoie R, Harel J. J Bacteriol 196 2944-2953 (2014)
  7. Comparative Pathogenomics of Escherichia coli: Polyvalent Vaccine Target Identification through Virulome Analysis. Clark JR, Maresso AM. Infect Immun 89 e0011521 (2021)
  8. Monitoring F1651 P-like fimbria expression at the single-cell level reveals a highly heterogeneous phenotype. Graveline R, Lavoie R, Garneau P, Daigle F, Sénéchal S, Martin C, Harel J. Infect Immun 83 1929-1939 (2015)


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