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ARN de doble hélice en el virus del mosaico del tabaco satélite
S B Larson1, S Koszelak, J Day
1Department of Biochemistry, University of California, Riverside 92521.
Nature
|January 14, 1993
Resumen
El virus del mosaico satélite del tabaco (STMV) tiene una estructura de cápside icosaédrica. La cristalografía de rayos X reveló que su proteína de capa contiene una proteína única.
Área de la Ciencia:
- Virología Virología.
- Biología Estructural Biología estructural.
- La bioquímica es la bioquímica.
Sus antecedentes:
- El virus del mosaico del tabaco satélite (STMV) es un virus esférico que depende del virus del mosaico del tabaco ayudante (TMV) para su replicación.
- STMV posee una cápside icosaédrica T=1 compuesta por 60 subunidades de proteínas y un genoma de ARN de una sola hebra.
- El STMV es estructuralmente distinto del STNV y no muestra homología con el STNV o el TMV.
Objetivo del estudio:
- Para determinar la estructura cristalina de rayos X de STMV.
- Para aclarar las características estructurales de la proteína cápside STMV y su interacción con el ARN genómico.
Principales métodos:
- Se empleó cristalografía de rayos X para determinar la estructura de alta resolución de STMV.
- El análisis estructural se centró en el pliegue de la proteína de la capa y las interacciones proteína-ácido nucleico dentro de la cápside.
Principales resultados:
- La proteína de la capa STMV presenta un dominio de barril beta "Swiss roll" con una cadena amino-terminal extendida crucial para las interacciones cuaternarias.
- Cada dímero de cápside está asociado con un segmento de doble hélice de ARN de siete pares de bases, con la díada del dímero coincidiendo con el par de bases central.
- Se observaron extensas interacciones proteína-ácido nucleico, y las hélices de ARN, con bases terminales 3' apiladas, se desvían de las formas canónicas.
Conclusiones:
- La estructura determinada proporciona información detallada sobre el montaje y la estabilidad de la cápside STMV.
- Las características estructurales únicas y las extensas interacciones de ARN resaltan nuevos mecanismos en la formación de cápsides virales y envasado del genoma.
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