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    csgA curlin, major subunit [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 949055, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    A gut bacterial amyloid promotes alpha-synuclein aggregation and motor impairment in mice.

    A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice.
    Sampson TR, Challis C, Jain N, Moiseyenko A, Ladinsky MS, Shastri GG, Thron T, Needham BD, Horvath I, Debelius JW, Janssen S, Knight R, Wittung-Stafshede P, Gradinaru V, Chapman M, Mazmanian SK., Free PMC Article

    04/3/2021
    NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.

    NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.
    Sewell L, Stylianou F, Xu Y, Taylor J, Sefer L, Matthews S., Free PMC Article

    12/5/2020
    Studies show the common structural features of CsgC and CsgE and the potential implications for general inhibition of amyloid.

    Structural insights into functional amyloid inhibition in Gram -ve bacteria.
    Hawthorne W, Rouse S, Sewell L, Matthews SJ., Free PMC Article

    07/22/2017
    CsgA deletion mutant lost its adherence to HTB-9 but continued to adhere to the HUVEC and Vero cells.

    Curli fimbria: an Escherichia coli adhesin associated with human cystitis.
    Cordeiro MA, Werle CH, Milanez GP, Yano T., Free PMC Article

    12/17/2016
    A Monte Carlo study of the early steps of functional amyloid formation of bacterial biofilm, which is primarily formed by aggregates of the protein CsgA, has been presented.

    A Monte Carlo Study of the Early Steps of Functional Amyloid Formation.
    Tian P, Lindorff-Larsen K, Boomsma W, Jensen MH, Otzen DE., Free PMC Article

    07/2/2016
    Inactivation of the cysH gene results in increased surface adhesion and cell aggregation by activating the expression of the curli-encoding csgBAC operon via phosphoadenosine 59-phosphosulfate accumulation.

    Sulfate assimilation pathway intermediate phosphoadenosine 59-phosphosulfate acts as a signal molecule affecting production of curli fibres in Escherichia coli.
    Rossi E, Motta S, Mauri P, Landini P.

    06/6/2015
    It was thus verified that the reinforcement of csgA gene in the DeltarpoS cells induced the enhanced colonization on the solid surfaces with the increased flagellum and curli expressions.

    Enhanced colonization of rpoS-deficient Escherichia coli cells on solid surfaces by reinforced csgA gene expression.
    Nguyen MH, Ojima Y, Taya M.

    05/30/2015
    Substoichiometric concentrations of CsgB induce a change in the mechanism of CsgA aggregation from that of forming amorphous aggregates to that of structured intermediates similar to those of CsgB alone

    The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism.
    Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C., Free PMC Article

    07/14/2012
    CsgA polymerization in vitro is preceded by the formation of thin needlelike protofibrils followed by aggregation of the amyloid fibrils.

    Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation.
    Dueholm MS, Nielsen SB, Hein KL, Nissen P, Chapman M, Christiansen G, Nielsen PH, Otzen DE., Free PMC Article

    12/10/2011
    Data describe aspartic acid and glycine residues that function as "gatekeepers" to modulate CsgA polymerization efficiency and potential toxicity.

    Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis.
    Wang X, Zhou Y, Ren JJ, Hammer ND, Chapman MR., Free PMC Article

    03/15/2010
    fibrils formed by CsgA and CsgB, the primary curli proteins of Escherichia coli, possess many of the hallmarks typical of amyloid

    The functional curli amyloid is not based on in-register parallel beta-sheet structure.
    Shewmaker F, McGlinchey RP, Thurber KR, McPhie P, Dyda F, Tycko R, Wickner RB., Free PMC Article

    01/21/2010
    Analysis of the influence of virulence and global regulators in the production of curli in EPEC identified Fis (factor for inversion stimulation) as a, heretofore unrecognized, negative transcriptional regulator of csgA expression.

    Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli.
    Saldaña Z, Xicohtencatl-Cortes J, Avelino F, Phillips AD, Kaper JB, Puente JL, Girón JA., Free PMC Article

    01/21/2010
    CsgD overexpression can overcome temperature-dependent control of the curli-encoding csgBA operon, but not of the cellulose-related adrA gene

    Cellulose modulates biofilm formation by counteracting curli-mediated colonization of solid surfaces in Escherichia coli.
    Gualdi L, Tagliabue L, Bertagnoli S, Ieranò T, De Castro C, Landini P.

    01/21/2010
    N-terminus verified by Edman degradation on mature peptideSee all PubMed (2) articles11/5/2007
    CsgB(trunc) was only able to act as a nucleator when cells were genetically manipulated to secrete higher concentrations of CsgA

    The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization.
    Hammer ND, Schmidt JC, Chapman MR., Free PMC Article

    01/21/2010
    At least three of five repeating units of CsgA are amyloidogenic, suggesting that covalent linkage of multiple amyloidogenic units facilitates efficient fiber formation.

    In vitro polymerization of a functional Escherichia coli amyloid protein.
    Wang X, Smith DR, Jones JW, Chapman MR., Free PMC Article

    01/21/2010
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