Continuous Assembly of β-Roll Structures Is Implicated in the
Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX)
Proteins

J 2020

Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins

MOTLOVA, Lucia; Nela KLIMOVA; Radovan FISER; Peter SEBO; Ladislav BUMBA et al.

Základní údaje

Originální název

Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins

Autoři

MOTLOVA, Lucia; Nela KLIMOVA; Radovan FISER; Peter SEBO a Ladislav BUMBA

Vydání

Journal of Molecular Biology, LONDON, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2020, 0022-2836

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.469

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90127/20:00139240

Organizační jednotka

CIISB II

Klíčová slova anglicky

PERTUSSIS ADENYLATE-CYCLASE; BORDETELLA-PERTUSSIS; CRYSTAL-STRUCTURE; FUNCTIONAL-CHARACTERIZATION; PSEUDOMONAS-AERUGINOSA; ESCHERICHIA-COLI; CALCIUMBINDINGPROTEASESYSTEM

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 29. 3. 2025 15:04, Mgr. Eva Dubská

Anotace

V originále

Repeats-in-Toxin (RTX) proteins of Gram-negative bacteria are excreted through the type I secretion system (T1SS) that recognizes non-cleavable C-terminal secretion signals. These are preceded by arrays of glycine and aspartate-rich nonapeptide repeats grouped by four to eight beta strands into blocks that fold into calcium binding parallel beta-roll structures. The beta-rolls are interspersed by linkers of variable length and sequence and the organization of multiple RTX repeat blocks within large RTX domains remains unknown. Here we examined the structure and function of the RTX domain of Bordetella pertussis adenylate cyclase toxin (CyaA) that is composed of five 6-roll RTX blocks. We show that the non-folded RTX repeats maintain the stability of the CyaA polypeptide in the Ca2+-depleted bacterial cytosol and thereby enable its efficient translocation through the Ti SS apparatus. The efficacy of secretion of truncated CyaA constructs was dictated by the number of retained RTX repeat blocks and depended on the presence of extracellular Ca2+ ions. We further describe the crystal structure of the RTX blocks IV-V of CyaA (CyaA(1372-1681)) that consists of a contiguous assembly of two beta-rolls that differs substantially from the arrangement of the RTX blocks observed in RTX lipases or other RTX proteins. These results provide a novel structural insight into the architecture of the RTX domains of large RTX proteins and support the "push-ratchet" mechanism of the T1SS-mediated secretion of very large RTX proteins. (C) 2020 Elsevier Ltd. All rights reserved.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

MOTLOVA, Lucia; Nela KLIMOVA; Radovan FISER; Peter SEBO a Ladislav BUMBA. Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. Journal of Molecular Biology. LONDON: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2020, roč. 432, č. 20, s. 5696-5710. ISSN 0022-2836. Dostupné z: https://doi.org/10.1016/j.jmb.2020.08.020.

@article{2487422,
   author = {Motlova, Lucia and Klimova, Nela and Fiser, Radovan and Sebo, Peter and Bumba, Ladislav},
   article_location = {LONDON},
   article_number = {20},
   doi = {https://doi.org/10.1016/j.jmb.2020.08.020},
   keywords = {PERTUSSIS ADENYLATE-CYCLASE; BORDETELLA-PERTUSSIS; CRYSTAL-STRUCTURE; FUNCTIONAL-CHARACTERIZATION; PSEUDOMONAS-AERUGINOSA; ESCHERICHIA-COLI; CALCIUMBINDINGPROTEASESYSTEM},
   language = {eng},
   issn = {0022-2836},
   journal = {Journal of Molecular Biology},
   title = {Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins},
   url = {https://www.sciencedirect.com/science/article/abs/pii/S0022283620305143?via%3Dihub},
   volume = {432},
   year = {2020}
}

TY  - JOUR
ID  - 2487422
AU  - Motlova, Lucia - Klimova, Nela - Fiser, Radovan - Sebo, Peter - Bumba, Ladislav
PY  - 2020
TI  - Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins
JF  - Journal of Molecular Biology
VL  - 432
IS  - 20
SP  - 5696-5710
EP  - 5696-5710
PB  - ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
SN  - 00222836
KW  - PERTUSSIS ADENYLATE-CYCLASE
KW  - BORDETELLA-PERTUSSIS
KW  - CRYSTAL-STRUCTURE
KW  - FUNCTIONAL-CHARACTERIZATION
KW  - PSEUDOMONAS-AERUGINOSA
KW  - ESCHERICHIA-COLI
KW  - CALCIUMBINDINGPROTEASESYSTEM
UR  - https://www.sciencedirect.com/science/article/abs/pii/S0022283620305143?via%3Dihub
N2  - Repeats-in-Toxin (RTX) proteins of Gram-negative bacteria are excreted through the type I secretion system (T1SS) that recognizes non-cleavable C-terminal secretion signals. These are preceded by arrays of glycine and aspartate-rich nonapeptide repeats grouped by four to eight beta strands into blocks that fold into calcium binding parallel beta-roll structures. The beta-rolls are interspersed by linkers of variable length and sequence and the organization of multiple RTX repeat blocks within large RTX domains remains unknown. Here we examined the structure and function of the RTX domain of Bordetella pertussis adenylate cyclase toxin (CyaA) that is composed of five 6-roll RTX blocks. We show that the non-folded RTX repeats maintain the stability of the CyaA polypeptide in the Ca2+-depleted bacterial cytosol and thereby enable its efficient translocation through the Ti SS apparatus. The efficacy of secretion of truncated CyaA constructs was dictated by the number of retained RTX repeat blocks and depended on the presence of extracellular Ca2+ ions. We further describe the crystal structure of the RTX blocks IV-V of CyaA (CyaA(1372-1681)) that consists of a contiguous assembly of two beta-rolls that differs substantially from the arrangement of the RTX blocks observed in RTX lipases or other RTX proteins. These results provide a novel structural insight into the architecture of the RTX domains of large RTX proteins and support the "push-ratchet" mechanism of the T1SS-mediated secretion of very large RTX proteins. (C) 2020 Elsevier Ltd. All rights reserved.
ER  -

MOTLOVA, Lucia; Nela KLIMOVA; Radovan FISER; Peter SEBO a Ladislav BUMBA. Continuous Assembly of β-Roll Structures Is Implicated in the Type I-Dependent Secretion of Large Repeat-in-Toxins (RTX) Proteins. \textit{Journal of Molecular Biology}. LONDON: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2020, roč.~432, č.~20, s.~5696-5710. ISSN~0022-2836. Dostupné z: https://doi.org/10.1016/j.jmb.2020.08.020.

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