KEZAR, A., L. KAVCIC, Martin POLÁK, Jiří NOVÁČEK, I. GUTIERREZ-AGUIRRE, M.T. ZNIDARIC, A. CO, K. STARE, K. GRUDEN, M. RAVNIKAR, D. PAHOVNIK, E. ZAGAR, F. MERZEL, G. ANDERLUH and M. PODOBNIK. Structural basis for the multitasking nature of the potato virus Y coat protein. Science advances. New York: American Association for the Advancement of Science, 2019, vol. 5, No 7, p. 1-13. ISSN 2375-2548. Available from: https://dx.doi.org/10.1126/sciadv.aaw3808.
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Basic information
Original name Structural basis for the multitasking nature of the potato virus Y coat protein
Authors KEZAR, A., L. KAVCIC, Martin POLÁK (203 Czech Republic, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, guarantor, belonging to the institution), I. GUTIERREZ-AGUIRRE, M.T. ZNIDARIC, A. CO, K. STARE, K. GRUDEN, M. RAVNIKAR, D. PAHOVNIK, E. ZAGAR, F. MERZEL, G. ANDERLUH and M. PODOBNIK.
Edition Science advances, New York, American Association for the Advancement of Science, 2019, 2375-2548.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 13.117
RIV identification code RIV/00216224:14740/19:00113326
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1126/sciadv.aaw3808
UT WoS 000478770400067
Keywords in English REAL-TIME PCR; CRYO-EM; PLANT-VIRUSES; POTYVIRUS; TERMINUS; ELECTROSTATICS; REFINEMENT; RESOLUTION; RESIDUES; PVYNTN
Tags CF CRYO, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Eva Dubská, učo 77638. Changed: 12/10/2023 09:13.
Abstract
Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY's flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA-coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein's amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.
Links
LM2015043, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
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