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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00533857" target="_blank" >RIV/61388971:_____/20:00533857 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/20:10421603

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0022283620305143" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0022283620305143</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jmb.2020.08.020" target="_blank" >10.1016/j.jmb.2020.08.020</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Molecular Biology

ISSN

0022-2836

e-ISSN

—

Volume of the periodical

432

Issue of the periodical within the volume

20

Country of publishing house

GB - UNITED KINGDOM

Number of pages

15

Pages from-to

5696-5710

UT code for WoS article

000576472300012

EID of the result in the Scopus database

2-s2.0-85090483661