Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression
We report the nucleotide sequence of human geranylgeranyl diphosphate (GGPP) synthase cDNA isolated from a fetal heart library. The 2.5 kb cDNA encodes a protein of 34 kDa. The protein contains six domains that have been identified previously in many other prenyltransferases. Recombinant, purified h...
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Format: | Article |
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Elsevier
1998-09-01
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Series: | Journal of Lipid Research |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520321593 |
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author | Johan Ericsson John M. Greene Kenneth C. Carter Brenda K. Shell D. Roxanne Duan Charles Florence Peter A. Edwards |
author_facet | Johan Ericsson John M. Greene Kenneth C. Carter Brenda K. Shell D. Roxanne Duan Charles Florence Peter A. Edwards |
author_sort | Johan Ericsson |
collection | DOAJ |
description | We report the nucleotide sequence of human geranylgeranyl diphosphate (GGPP) synthase cDNA isolated from a fetal heart library. The 2.5 kb cDNA encodes a protein of 34 kDa. The protein contains six domains that have been identified previously in many other prenyltransferases. Recombinant, purified histidine-tagged protein exhibited the enzymatic properties associated with GGPP synthase, namely the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosphate. Transient transfection of mammalian cells with a plasmid encoding the putative GGPP synthase resulted in a 55-fold increase in GGPP synthase activity. Taken together, these results establish that the cDNA encodes the mammalian GGPP synthase protein. The mRNA for GGPP synthase was expressed ubiquitiously. Of the 16 human tissues examined, the highest expression of the mRNA was in testis. The mRNA levels in cultured HeLa cells were unaffected by alterations in cellular sterol levels and contrasted with the significant regulation of isopentenyl diphosphate synthase mRNA under these same conditions. Fluorescent in situ hybridization was used to map the single gene encoding human GGPP synthase to chromosome 1q43.—Ericsson, J., J. M. Greene, K. C. Carter, B. K. Shell, D. R. Duan, C. Florence, and P. A. Edwards. Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping, and tissue expression. |
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issn | 0022-2275 |
language | English |
last_indexed | 2024-12-20T12:10:05Z |
publishDate | 1998-09-01 |
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spelling | doaj.art-d2311d0917744433a4eae5e16c96697a2022-12-21T19:41:16ZengElsevierJournal of Lipid Research0022-22751998-09-0139917311739Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expressionJohan Ericsson0John M. Greene1Kenneth C. Carter2Brenda K. Shell3D. Roxanne Duan4Charles Florence5Peter A. Edwards6Departments of Biological Chemistry, University of California Los Angeles, Los Angeles, CA 90095; Medicine, University of California Los Angeles, Los Angeles, CA 90095Human Genome Sciences, Bioinformatics, 9410 Key West Avenue, Rockville, MD 20850Human Genome Sciences, Bioinformatics, 9410 Key West Avenue, Rockville, MD 20850Human Genome Sciences, Bioinformatics, 9410 Key West Avenue, Rockville, MD 20850Human Genome Sciences, Bioinformatics, 9410 Key West Avenue, Rockville, MD 20850Human Genome Sciences, Bioinformatics, 9410 Key West Avenue, Rockville, MD 20850To whom correspondence should be addressed.; Departments of Biological Chemistry, University of California Los Angeles, Los Angeles, CA 90095; Medicine, University of California Los Angeles, Los Angeles, CA 90095; the Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095We report the nucleotide sequence of human geranylgeranyl diphosphate (GGPP) synthase cDNA isolated from a fetal heart library. The 2.5 kb cDNA encodes a protein of 34 kDa. The protein contains six domains that have been identified previously in many other prenyltransferases. Recombinant, purified histidine-tagged protein exhibited the enzymatic properties associated with GGPP synthase, namely the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosphate. Transient transfection of mammalian cells with a plasmid encoding the putative GGPP synthase resulted in a 55-fold increase in GGPP synthase activity. Taken together, these results establish that the cDNA encodes the mammalian GGPP synthase protein. The mRNA for GGPP synthase was expressed ubiquitiously. Of the 16 human tissues examined, the highest expression of the mRNA was in testis. The mRNA levels in cultured HeLa cells were unaffected by alterations in cellular sterol levels and contrasted with the significant regulation of isopentenyl diphosphate synthase mRNA under these same conditions. Fluorescent in situ hybridization was used to map the single gene encoding human GGPP synthase to chromosome 1q43.—Ericsson, J., J. M. Greene, K. C. Carter, B. K. Shell, D. R. Duan, C. Florence, and P. A. Edwards. Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping, and tissue expression.http://www.sciencedirect.com/science/article/pii/S0022227520321593prenyltransferase |
spellingShingle | Johan Ericsson John M. Greene Kenneth C. Carter Brenda K. Shell D. Roxanne Duan Charles Florence Peter A. Edwards Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression Journal of Lipid Research prenyltransferase |
title | Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression |
title_full | Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression |
title_fullStr | Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression |
title_full_unstemmed | Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression |
title_short | Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression |
title_sort | human geranylgeranyl diphosphate synthase isolation of the cdna chromosomal mapping and tissue expression |
topic | prenyltransferase |
url | http://www.sciencedirect.com/science/article/pii/S0022227520321593 |
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