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Isolation and Sequencing of a Plant cDNA Encoding a Bifunctional Methylenetetrahydrofolate Dehydrogenase : Methenyltetrahydrofolate Cyclohydrolase Protein

Isolation and Sequencing of a Plant cDNA Encoding a Bifunctional Methylenetetrahydrofolate... Summary In plant cells, the interconversion of formyl- and methylene-tetrahydrofolates is catalyzed by a bifunctional protein possessing methenyltetrallydrofolate cydohydrolase (EC 3.5.4.9) and methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5) activities. The present work reports the isolation and sequencing of a cDNA that encodes this protein. Polydonal antibodies, raised against purified pea cytosolic dehydrogenase:cyclohydrolase, were used to screen a λgt 11 cDNA expression library, constructed from leaf extracts of this species. The screen identified a phage containing a cDNA insert with an open reading frame encoding a 294 amino acid protein (M r 31,344). The deduced primary structure of this protein contained most of the conserved regions found in other dehydrogenase:cyclohydrolase proteins including the corresponding domains of the trifunctional C 1 -THF synthases of mammalian and yeast origins. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Pteridines de Gruyter

Isolation and Sequencing of a Plant cDNA Encoding a Bifunctional Methylenetetrahydrofolate Dehydrogenase : Methenyltetrahydrofolate Cyclohydrolase Protein

Pteridines , Volume 10 (4) – Nov 1, 1999

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References (28)

Publisher
de Gruyter
Copyright
Copyright © 1999 by the
ISSN
0933-4807
eISSN
2195-4720
DOI
10.1515/pteridines.1999.10.4.171
Publisher site
See Article on Publisher Site

Abstract

Summary In plant cells, the interconversion of formyl- and methylene-tetrahydrofolates is catalyzed by a bifunctional protein possessing methenyltetrallydrofolate cydohydrolase (EC 3.5.4.9) and methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5) activities. The present work reports the isolation and sequencing of a cDNA that encodes this protein. Polydonal antibodies, raised against purified pea cytosolic dehydrogenase:cyclohydrolase, were used to screen a λgt 11 cDNA expression library, constructed from leaf extracts of this species. The screen identified a phage containing a cDNA insert with an open reading frame encoding a 294 amino acid protein (M r 31,344). The deduced primary structure of this protein contained most of the conserved regions found in other dehydrogenase:cyclohydrolase proteins including the corresponding domains of the trifunctional C 1 -THF synthases of mammalian and yeast origins.

Journal

Pteridinesde Gruyter

Published: Nov 1, 1999

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