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. |
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@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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