Structure and genome release of Twort-like Myoviridae phage
with a double-layered baseplate

J 2016

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

NOVÁČEK, Jiří, Marta ŠIBOROVÁ, Martin BENEŠÍK, Roman PANTŮČEK, Jiří DOŠKAŘ et. al.

Základní údaje

Originální název

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Autoři

NOVÁČEK, Jiří (203 Česká republika, domácí), Marta ŠIBOROVÁ (203 Česká republika, domácí), Martin BENEŠÍK (203 Česká republika, domácí), Roman PANTŮČEK (203 Česká republika, domácí), Jiří DOŠKAŘ (203 Česká republika, domácí) a Pavel PLEVKA (203 Česká republika, garant, domácí)

Vydání

Proceedings of the National Academy of Sciences of the United States of America, WASHINGTON, National Academy of Sciences, 2016, 0027-8424

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 9.661

Kód RIV

RIV/00216224:14740/16:00088711

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1073/pnas.1605883113

UT WoS

000381399200067

Klíčová slova anglicky

bacteriophage; structure; contraction; Staphylococcus; genome release

Štítky

CF CRYO, rivok

Změněno: 27. 2. 2019 11:43, prof. RNDr. Roman Pantůček, Ph.D.

Anotace

V originále

Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with "double-layered" baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210 degrees rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome's release.

Návaznosti

GJ15-21631Y, projekt VaV

Název: Strukturní studie potenciálního protibakteriálního agens, fága 812K1-420 infikujícího zlatého stafylokoka

Investor: Grantová agentura ČR, Strukturní studie potenciálního protibakteriálního agens, fága 812K1-420 infikujícího zlatého stafylokoka

LM2010005, projekt VaV

Název: Velká infrastruktura CESNET (Akronym: VI CESNET)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Velká infrastruktura CESNET

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

NOVÁČEK, Jiří, Marta ŠIBOROVÁ, Martin BENEŠÍK, Roman PANTŮČEK, Jiří DOŠKAŘ a Pavel PLEVKA. Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate. Proceedings of the National Academy of Sciences of the United States of America. WASHINGTON: National Academy of Sciences, 2016, roč. 113, č. 33, s. 9351-9356. ISSN 0027-8424. Dostupné z: https://dx.doi.org/10.1073/pnas.1605883113.

@article{1373954,
   author = {Nováček, Jiří and Šiborová, Marta and Benešík, Martin and Pantůček, Roman and Doškař, Jiří and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {33},
   doi = {http://dx.doi.org/10.1073/pnas.1605883113},
   keywords = {bacteriophage; structure; contraction; Staphylococcus; genome release},
   language = {eng},
   issn = {0027-8424},
   journal = {Proceedings of the National Academy of Sciences of the United States of America},
   title = {Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate},
   url = {http://www.pnas.org/content/113/33/9351},
   volume = {113},
   year = {2016}
}

TY  - JOUR
ID  - 1373954
AU  - Nováček, Jiří - Šiborová, Marta - Benešík, Martin - Pantůček, Roman - Doškař, Jiří - Plevka, Pavel
PY  - 2016
TI  - Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate
JF  - Proceedings of the National Academy of Sciences of the United States of America
VL  - 113
IS  - 33
SP  - 9351-9356
EP  - 9351-9356
PB  - National Academy of Sciences
SN  - 00278424
KW  - bacteriophage
KW  - structure
KW  - contraction
KW  - Staphylococcus
KW  - genome release
UR  - http://www.pnas.org/content/113/33/9351
L2  - http://www.pnas.org/content/113/33/9351
N2  - Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with "double-layered" baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210 degrees rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome's release.
ER  -

NOVÁČEK, Jiří, Marta ŠIBOROVÁ, Martin BENEŠÍK, Roman PANTŮČEK, Jiří DOŠKAŘ a Pavel PLEVKA. Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate. \textit{Proceedings of the National Academy of Sciences of the United States of America}. WASHINGTON: National Academy of Sciences, 2016, roč.~113, č.~33, s.~9351-9356. ISSN~0027-8424. Dostupné z: https://dx.doi.org/10.1073/pnas.1605883113.

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