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The Sec2 translocase of the chloroplast inner envelope contains a unique and dedicated SECE2 component.
Li, Yubing; Singhal, Rajneesh; Taylor, Isaiah W; McMinn, Patrick H; Chua, Xien Yu; Cline, Kenneth; Fernandez, Donna E.
Afiliación
  • Li Y; Horticultural Sciences Department and Plant Molecular and Cellular Biology, University of Florida, Gainesville, FL, 32611, USA.
  • Singhal R; Department of Botany, University of Wisconsin at Madison, 430 Lincoln Drive, Madison, WI, 53706, USA.
  • Taylor IW; Department of Botany, University of Wisconsin at Madison, 430 Lincoln Drive, Madison, WI, 53706, USA.
  • McMinn PH; Department of Botany, University of Wisconsin at Madison, 430 Lincoln Drive, Madison, WI, 53706, USA.
  • Chua XY; Department of Botany, University of Wisconsin at Madison, 430 Lincoln Drive, Madison, WI, 53706, USA.
  • Cline K; Horticultural Sciences Department and Plant Molecular and Cellular Biology, University of Florida, Gainesville, FL, 32611, USA.
  • Fernandez DE; Department of Botany, University of Wisconsin at Madison, 430 Lincoln Drive, Madison, WI, 53706, USA.
Plant J ; 84(4): 647-58, 2015 Nov.
Article en En | MEDLINE | ID: mdl-26406904
ABSTRACT
Biogenesis of chloroplasts involves a series of protein trafficking events. Nuclear-encoded proteins are imported into the organelle, and then trafficked to various chloroplast locations by systems that are directly homologous to bacterial systems. Although the thylakoid-based systems have been studied extensively, much less is known about the systems that reside and function in the inner envelope membrane. One such system, the Sec2 system, is homologous to both the thylakoid-based Sec1 system and bacterial Sec systems, and may mediate both integration and translocation across the inner envelope. At a minimum, this system is expected to include three components, but only two, SCY2 and SECA2, have been identified in Arabidopsis. Bioinformatics and protein modeling were used to identify the protein encoded by At4g38490 as a candidate for the missing component (SECE2). Cellular localization, biochemistry, protein interaction assays in yeast, and co-immunoprecipitation experiments were used to establish that this protein is an integral membrane protein of the inner envelope, and specifically interacts with the SCY2 component in vivo. Sequence analyses indicated that SECE2 proteins are found in a variety of plants, and differ from the thylakoid SECE1 proteins in a stroma-exposed helical domain, which may contribute to their specificity. Finally, a genetic analysis indicated that SECE2 plays an essential role in plant growth and development.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Cloroplastos / Tilacoides / Proteínas de Arabidopsis / Proteínas de Cloroplastos / Proteínas de la Membrana Idioma: En Revista: Plant J Asunto de la revista: BIOLOGIA MOLECULAR / BOTANICA Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Cloroplastos / Tilacoides / Proteínas de Arabidopsis / Proteínas de Cloroplastos / Proteínas de la Membrana Idioma: En Revista: Plant J Asunto de la revista: BIOLOGIA MOLECULAR / BOTANICA Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos