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Sucrose synthase localizes to cellulose synthesis sites in tracheary elements.
Salnikov, V V; Grimson, M J; Delmer, D P; Haigler, C H.
Afiliación
  • Salnikov VV; Department of Biological Sciences, Texas Tech University, Box 43131, Lubbock, TX 79409, USA.
Phytochemistry ; 57(6): 823-33, 2001 Jul.
Article en En | MEDLINE | ID: mdl-11423134
ABSTRACT
The synthesis of crystalline cellulose microfibrils in plants is a highly coordinated process that occurs at the interface of the cortex, plasma membrane, and cell wall. There is evidence that cellulose biogenesis is facilitated by the interaction of several proteins, but the details are just beginning to be understood. In particular, sucrose synthase, microtubules, and actin have been proposed to possibly associate with cellulose synthases (microfibril terminal complexes) in the plasma membrane. Differentiating tracheary elements of Zinnia elegans L. were used as a model system to determine the localization of sucrose synthase and actin in relation to the plasma membrane and its underlying microtubules during the deposition of patterned, cellulose-rich secondary walls. Cortical actin occurs with similar density both between and under secondary wall thickenings. In contrast, sucrose synthase is highly enriched near the plasma membrane and the microtubules under the secondary wall thickenings. Both actin and sucrose synthase lie closer to the plasma membrane than the microtubules. These results show that the preferential localization of sucrose synthase at sites of high-rate cellulose synthesis can be generalized beyond cotton fibers, and they establish a spatial context for further work on a multi-protein complex that may facilitate secondary wall cellulose synthesis.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Celulosa / Asteraceae / Glucosiltransferasas Idioma: En Revista: Phytochemistry Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Celulosa / Asteraceae / Glucosiltransferasas Idioma: En Revista: Phytochemistry Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos