Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F19%3A00113245" target="_blank" >RIV/00216224:14740/19:00113245 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1038/s41564-019-0477-7" target="_blank" >http://dx.doi.org/10.1038/s41564-019-0477-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41564-019-0477-7" target="_blank" >10.1038/s41564-019-0477-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

Popis výsledku v původním jazyce

Phage tail fibres are elongated protein assemblies capable of specific recognition of bacterial surfaces during the first step of viral infection(1-4). The folding of these complex trimeric structures often requires a phage-encoded tail fibre assembly (Tfa) proteins(5-7). Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu. We demonstrate that Tfa forms a stable complex with the tail fibre, and present a 2.1 angstrom resolution X-ray crystal structure of this complex. We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that probably mediates fibre oligomerization and assembly. Tfa forms rapidly exchanging multimers on its own, but not a stable trimer, implying that Tfa does not specify the trimeric state of the fibre. We propose that the key conserved role of Tfa is to ensure that fibre assembly and multimerization initiates at the C terminus, ensuring that the intertwined and repetitive structural elements of fibres come together in the correct sequence. The universal importance of correctly aligning the C termini of phage fibres is highlighted by our work.

Název v anglickém jazyce

Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

Popis výsledku anglicky

Phage tail fibres are elongated protein assemblies capable of specific recognition of bacterial surfaces during the first step of viral infection(1-4). The folding of these complex trimeric structures often requires a phage-encoded tail fibre assembly (Tfa) proteins(5-7). Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu. We demonstrate that Tfa forms a stable complex with the tail fibre, and present a 2.1 angstrom resolution X-ray crystal structure of this complex. We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that probably mediates fibre oligomerization and assembly. Tfa forms rapidly exchanging multimers on its own, but not a stable trimer, implying that Tfa does not specify the trimeric state of the fibre. We propose that the key conserved role of Tfa is to ensure that fibre assembly and multimerization initiates at the C terminus, ensuring that the intertwined and repetitive structural elements of fibres come together in the correct sequence. The universal importance of correctly aligning the C termini of phage fibres is highlighted by our work.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10606 - Microbiology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Nature Microbiology

ISSN

2058-5276

e-ISSN

—

Svazek periodika

4

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

1645-1653

Kód UT WoS článku

000487286800010

EID výsledku v databázi Scopus

2-s2.0-85068091527