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Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Standard

Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. / Rasmussen, Casper B.; Christiansen, Gunna; Vad, Brian S. et al.
I: Protein Science, Bind 28, Nr. 3, 01.03.2019, s. 633-642.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Rasmussen, CB, Christiansen, G, Vad, BS, Lynggaard, C, Enghild, JJ, Andreasen, M & Otzen, D 2019, 'Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation', Protein Science, bind 28, nr. 3, s. 633-642. https://doi.org/10.1002/pro.3566

APA

Rasmussen, C. B., Christiansen, G., Vad, B. S., Lynggaard, C., Enghild, J. J., Andreasen, M., & Otzen, D. (2019). Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science, 28(3), 633-642. https://doi.org/10.1002/pro.3566

CBE

Rasmussen CB, Christiansen G, Vad BS, Lynggaard C, Enghild JJ, Andreasen M, Otzen D. 2019. Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science. 28(3):633-642. https://doi.org/10.1002/pro.3566

MLA

Rasmussen, Casper B. et al. "Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation". Protein Science. 2019, 28(3). 633-642. https://doi.org/10.1002/pro.3566

Vancouver

Rasmussen CB, Christiansen G, Vad BS, Lynggaard C, Enghild JJ, Andreasen M et al. Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. Protein Science. 2019 mar. 1;28(3):633-642. doi: 10.1002/pro.3566

Author

Rasmussen, Casper B. ; Christiansen, Gunna ; Vad, Brian S. et al. / Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation. I: Protein Science. 2019 ; Bind 28, Nr. 3. s. 633-642.

Bibtex

@article{ea73778c11734802bbf329e9b9aa2718,
title = "Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation",
abstract = "Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be reflected in the aggregation mechanism. FA from different bacteria, including Escherichia coli (CsgA) and Pseudomonas (FapC), contains a number of imperfect repeats which may be key to efficient aggregation. Here we report on the aggregative behavior of FapC constructs which represent all single, double, and triple deletions of the protein's three imperfect repeats. Analysis of the fibrillation kinetics by the program Amylofit reveals that the removal of these repeats increases the tendency of the growing fibrils to fragment and also generally increases aggregation half-times. Remarkably, even the mutant lacking all three repeats was able to fibrillate, although fibrillation was much more irregular and led to significantly altered and destabilized fibrils. We conclude that imperfect repeats can promote fibrillation efficiency thanks to their modular design, though the context of the imperfect repeats also plays a significant role.",
keywords = "aggregation mechanisms, Amylofit, FapC, kinetic analysis, Thioflavin T",
author = "Rasmussen, {Casper B.} and Gunna Christiansen and Vad, {Brian S.} and Carina Lynggaard and Enghild, {Jan J.} and Maria Andreasen and Daniel Otzen",
year = "2019",
month = mar,
day = "1",
doi = "10.1002/pro.3566",
language = "English",
volume = "28",
pages = "633--642",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell Publishing, Inc.",
number = "3",

}

RIS

TY - JOUR

T1 - Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation

AU - Rasmussen, Casper B.

AU - Christiansen, Gunna

AU - Vad, Brian S.

AU - Lynggaard, Carina

AU - Enghild, Jan J.

AU - Andreasen, Maria

AU - Otzen, Daniel

PY - 2019/3/1

Y1 - 2019/3/1

N2 - Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be reflected in the aggregation mechanism. FA from different bacteria, including Escherichia coli (CsgA) and Pseudomonas (FapC), contains a number of imperfect repeats which may be key to efficient aggregation. Here we report on the aggregative behavior of FapC constructs which represent all single, double, and triple deletions of the protein's three imperfect repeats. Analysis of the fibrillation kinetics by the program Amylofit reveals that the removal of these repeats increases the tendency of the growing fibrils to fragment and also generally increases aggregation half-times. Remarkably, even the mutant lacking all three repeats was able to fibrillate, although fibrillation was much more irregular and led to significantly altered and destabilized fibrils. We conclude that imperfect repeats can promote fibrillation efficiency thanks to their modular design, though the context of the imperfect repeats also plays a significant role.

AB - Functional amyloid (FA) is widespread in bacteria and serves multiple purposes such as strengthening of biofilm and contact with eukaryotic hosts. Unlike pathological amyloid, FA has been subjected to evolutionary optimization which is likely to be reflected in the aggregation mechanism. FA from different bacteria, including Escherichia coli (CsgA) and Pseudomonas (FapC), contains a number of imperfect repeats which may be key to efficient aggregation. Here we report on the aggregative behavior of FapC constructs which represent all single, double, and triple deletions of the protein's three imperfect repeats. Analysis of the fibrillation kinetics by the program Amylofit reveals that the removal of these repeats increases the tendency of the growing fibrils to fragment and also generally increases aggregation half-times. Remarkably, even the mutant lacking all three repeats was able to fibrillate, although fibrillation was much more irregular and led to significantly altered and destabilized fibrils. We conclude that imperfect repeats can promote fibrillation efficiency thanks to their modular design, though the context of the imperfect repeats also plays a significant role.

KW - aggregation mechanisms

KW - Amylofit

KW - FapC

KW - kinetic analysis

KW - Thioflavin T

UR - http://www.scopus.com/inward/record.url?scp=85059905643&partnerID=8YFLogxK

U2 - 10.1002/pro.3566

DO - 10.1002/pro.3566

M3 - Journal article

C2 - 30592554

AN - SCOPUS:85059905643

VL - 28

SP - 633

EP - 642

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 3

ER -