author_facet De Caroli, Monica
Lenucci, Marcello S.
Di Sansebastiano, Gian-Pietro
Tunno, Michela
Montefusco, Anna
Dalessandro, Giuseppe
Piro, Gabriella
De Caroli, Monica
Lenucci, Marcello S.
Di Sansebastiano, Gian-Pietro
Tunno, Michela
Montefusco, Anna
Dalessandro, Giuseppe
Piro, Gabriella
author De Caroli, Monica
Lenucci, Marcello S.
Di Sansebastiano, Gian-Pietro
Tunno, Michela
Montefusco, Anna
Dalessandro, Giuseppe
Piro, Gabriella
spellingShingle De Caroli, Monica
Lenucci, Marcello S.
Di Sansebastiano, Gian-Pietro
Tunno, Michela
Montefusco, Anna
Dalessandro, Giuseppe
Piro, Gabriella
The Scientific World Journal
Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
General Environmental Science
General Biochemistry, Genetics and Molecular Biology
General Medicine
author_sort de caroli, monica
spelling De Caroli, Monica Lenucci, Marcello S. Di Sansebastiano, Gian-Pietro Tunno, Michela Montefusco, Anna Dalessandro, Giuseppe Piro, Gabriella 2356-6140 1537-744X Hindawi Limited General Environmental Science General Biochemistry, Genetics and Molecular Biology General Medicine http://dx.doi.org/10.1155/2014/792420 <jats:p><jats:italic>Cellulose synthase</jats:italic>-<jats:italic>like</jats:italic>(<jats:italic>Csl</jats:italic>) genes are believed to encode enzymes for the synthesis of cell wall matrix polysaccharides. The subfamily of<jats:italic>CslA</jats:italic>is putatively involved in the biosynthesis of<jats:italic>β</jats:italic>-mannans. Here we report a study on the cellular localization and the enzyme activity of an<jats:italic>Arabidopsis</jats:italic>CslA family member, AtCslA2. We show that the fluorescent protein fusion AtCslA2-GFP, transiently expressed in tobacco leaf protoplasts, is synthesized in the ER and it accumulates in the Golgi stacks. The chimera is inserted in the Golgi membrane and is functional since membrane preparations obtained by transformed protoplasts carry out the<jats:italic>in vitro</jats:italic>synthesis of a<jats:sup>14</jats:sup>C-mannan starting from GDP-<jats:sc>d</jats:sc>-[U-<jats:sup>14</jats:sup>C]mannose as substrate. The enzyme specific activity is increased by approximately 38% in the transformed protoplasts with respect to wild-type. Preliminary tests with proteinase K, biochemical data, and TM domain predictions suggest that the catalytic site of AtCslA2 faces the Golgi lumen.</jats:p> Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion of<i>Arabidopsis</i>Cellulose Synthase-Like A2 Inserted into Golgi Membrane The Scientific World Journal
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series The Scientific World Journal
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title Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_unstemmed Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_full Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_fullStr Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_full_unstemmed Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_short Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_sort cellular localization and biochemical characterization of a chimeric fluorescent protein fusion of<i>arabidopsis</i>cellulose synthase-like a2 inserted into golgi membrane
topic General Environmental Science
General Biochemistry, Genetics and Molecular Biology
General Medicine
url http://dx.doi.org/10.1155/2014/792420
publishDate 2014
physical 1-7
description <jats:p><jats:italic>Cellulose synthase</jats:italic>-<jats:italic>like</jats:italic>(<jats:italic>Csl</jats:italic>) genes are believed to encode enzymes for the synthesis of cell wall matrix polysaccharides. The subfamily of<jats:italic>CslA</jats:italic>is putatively involved in the biosynthesis of<jats:italic>β</jats:italic>-mannans. Here we report a study on the cellular localization and the enzyme activity of an<jats:italic>Arabidopsis</jats:italic>CslA family member, AtCslA2. We show that the fluorescent protein fusion AtCslA2-GFP, transiently expressed in tobacco leaf protoplasts, is synthesized in the ER and it accumulates in the Golgi stacks. The chimera is inserted in the Golgi membrane and is functional since membrane preparations obtained by transformed protoplasts carry out the<jats:italic>in vitro</jats:italic>synthesis of a<jats:sup>14</jats:sup>C-mannan starting from GDP-<jats:sc>d</jats:sc>-[U-<jats:sup>14</jats:sup>C]mannose as substrate. The enzyme specific activity is increased by approximately 38% in the transformed protoplasts with respect to wild-type. Preliminary tests with proteinase K, biochemical data, and TM domain predictions suggest that the catalytic site of AtCslA2 faces the Golgi lumen.</jats:p>
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author De Caroli, Monica, Lenucci, Marcello S., Di Sansebastiano, Gian-Pietro, Tunno, Michela, Montefusco, Anna, Dalessandro, Giuseppe, Piro, Gabriella
author_facet De Caroli, Monica, Lenucci, Marcello S., Di Sansebastiano, Gian-Pietro, Tunno, Michela, Montefusco, Anna, Dalessandro, Giuseppe, Piro, Gabriella, De Caroli, Monica, Lenucci, Marcello S., Di Sansebastiano, Gian-Pietro, Tunno, Michela, Montefusco, Anna, Dalessandro, Giuseppe, Piro, Gabriella
author_sort de caroli, monica
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container_title The Scientific World Journal
container_volume 2014
description <jats:p><jats:italic>Cellulose synthase</jats:italic>-<jats:italic>like</jats:italic>(<jats:italic>Csl</jats:italic>) genes are believed to encode enzymes for the synthesis of cell wall matrix polysaccharides. The subfamily of<jats:italic>CslA</jats:italic>is putatively involved in the biosynthesis of<jats:italic>β</jats:italic>-mannans. Here we report a study on the cellular localization and the enzyme activity of an<jats:italic>Arabidopsis</jats:italic>CslA family member, AtCslA2. We show that the fluorescent protein fusion AtCslA2-GFP, transiently expressed in tobacco leaf protoplasts, is synthesized in the ER and it accumulates in the Golgi stacks. The chimera is inserted in the Golgi membrane and is functional since membrane preparations obtained by transformed protoplasts carry out the<jats:italic>in vitro</jats:italic>synthesis of a<jats:sup>14</jats:sup>C-mannan starting from GDP-<jats:sc>d</jats:sc>-[U-<jats:sup>14</jats:sup>C]mannose as substrate. The enzyme specific activity is increased by approximately 38% in the transformed protoplasts with respect to wild-type. Preliminary tests with proteinase K, biochemical data, and TM domain predictions suggest that the catalytic site of AtCslA2 faces the Golgi lumen.</jats:p>
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spelling De Caroli, Monica Lenucci, Marcello S. Di Sansebastiano, Gian-Pietro Tunno, Michela Montefusco, Anna Dalessandro, Giuseppe Piro, Gabriella 2356-6140 1537-744X Hindawi Limited General Environmental Science General Biochemistry, Genetics and Molecular Biology General Medicine http://dx.doi.org/10.1155/2014/792420 <jats:p><jats:italic>Cellulose synthase</jats:italic>-<jats:italic>like</jats:italic>(<jats:italic>Csl</jats:italic>) genes are believed to encode enzymes for the synthesis of cell wall matrix polysaccharides. The subfamily of<jats:italic>CslA</jats:italic>is putatively involved in the biosynthesis of<jats:italic>β</jats:italic>-mannans. Here we report a study on the cellular localization and the enzyme activity of an<jats:italic>Arabidopsis</jats:italic>CslA family member, AtCslA2. We show that the fluorescent protein fusion AtCslA2-GFP, transiently expressed in tobacco leaf protoplasts, is synthesized in the ER and it accumulates in the Golgi stacks. The chimera is inserted in the Golgi membrane and is functional since membrane preparations obtained by transformed protoplasts carry out the<jats:italic>in vitro</jats:italic>synthesis of a<jats:sup>14</jats:sup>C-mannan starting from GDP-<jats:sc>d</jats:sc>-[U-<jats:sup>14</jats:sup>C]mannose as substrate. The enzyme specific activity is increased by approximately 38% in the transformed protoplasts with respect to wild-type. Preliminary tests with proteinase K, biochemical data, and TM domain predictions suggest that the catalytic site of AtCslA2 faces the Golgi lumen.</jats:p> Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion of<i>Arabidopsis</i>Cellulose Synthase-Like A2 Inserted into Golgi Membrane The Scientific World Journal
spellingShingle De Caroli, Monica, Lenucci, Marcello S., Di Sansebastiano, Gian-Pietro, Tunno, Michela, Montefusco, Anna, Dalessandro, Giuseppe, Piro, Gabriella, The Scientific World Journal, Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane, General Environmental Science, General Biochemistry, Genetics and Molecular Biology, General Medicine
title Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_full Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_fullStr Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_full_unstemmed Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_short Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
title_sort cellular localization and biochemical characterization of a chimeric fluorescent protein fusion of<i>arabidopsis</i>cellulose synthase-like a2 inserted into golgi membrane
title_unstemmed Cellular Localization and Biochemical Characterization of a Chimeric Fluorescent Protein Fusion ofArabidopsisCellulose Synthase-Like A2 Inserted into Golgi Membrane
topic General Environmental Science, General Biochemistry, Genetics and Molecular Biology, General Medicine
url http://dx.doi.org/10.1155/2014/792420