A Plant Virus Movement Protein Forms Ringlike Complexes with the Major Nucleolar Protein, Fibrillarin, In Vitro (Record no. 49095)

MARC details
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fixed length control field 02379nam a2200301Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625153950.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-14911
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Title A Plant Virus Movement Protein Forms Ringlike Complexes with the Major Nucleolar Protein, Fibrillarin, In Vitro
490 0# - SERIES STATEMENT
Volume/sequential designation J. Mol. Biol., 376, p.932-937, 2008
520 3# - SUMMARY, ETC.
Summary, etc. Fibrillarin, one of the major proteins of the nucleolus, has methyltransferase activity directing 2'-O-ribose methylation of rRNA and snRNAs and is required for rRNA processing. The ability of the plant umbravirus, groundnut rosette virus, to move long distances through the phloem, the specialized plant vascular system, has been shown to strictly depend on the interaction of one of its proteins, the ORF3 protein (protein encoded by open reading frame 3), with fibrillarin. This interaction is essential for several stages in the groundnut rosette virus life cycle such as nucleolar import of the ORF3 proteinviaCajal bodies, relocalization of some fibrillarin from the nucleolus to cytoplasm, and assembly of cytoplasmic umbraviral ribonu-cleoprotein particles that are themselves required for the long-distance spread of the virus and systemic infection. Here, using atomic force microscopy, we determine the architecture of these complexes as single-layered ringlike structures with a diameter of 18-22 nm and a height of 2.0±0.4 nm, which consist of several (n=6-8)distinct protein granules. We also estimate the molar ratio of fibrillarin to ORF3 protein in the complexes as approximately 1:1. Based on these data, we propose a model of the structural organization of fibrillarin-ORF3 protein complexes and discuss potential mechanistic and functional implications that may also apply to other viruses.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element ATOMIC FORCE MICROSCOPY
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element FIBRILLARIN; UMBRAVIRUS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element VIRUS MOVE-MENT
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PROTEIN COMPLEXES
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Canetta, E.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Kim, S.H.
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Personal name Kalinina, N.O.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Shaw, J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Adya, A.K.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Gillespie, T.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Brown, J.W.S.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Brown, J.W.S.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1bn11SLCpHOlY1NHLqxvQWi7NbH99Zzy8/view?usp=drivesdk">https://drive.google.com/file/d/1bn11SLCpHOlY1NHLqxvQWi7NbH99Zzy8/view?usp=drivesdk</a>
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Source of classification or shelving scheme Clasificación local
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-14911 25.06.2025 25.06.2025 Documentos solicitados